Aspartic Proteinases and Their Inhibitors : : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 / / Vladimír Kostka, Federation of European Biochemical Societies.

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spelling Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 / Vladimír Kostka, Federation of European Biochemical Societies.
Reprint 2015
Berlin ; Boston : De Gruyter, [2016]
©1985
1 online resource (613 p.) : Zahlr. Abb.
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computer c rdamedia
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Frontmatter -- Preface -- Acknowledgements -- Organizing Committee -- Contents -- Introduction -- Aspartic proteinases and their inhibitors / Kay, John -- Comments on the nomenclature of aspartic proteinases / Foltmann, Bent -- General aspartic proteinases -- Isolation, molecufer characteristics, and primary structures. Fungal aspartyl proteinases / Stepanov, Valentin M. -- Structure and properties of proteinase a from Saccharomyces carlsbergensis and Saccharomyces cerevisiae / Dreyer, Thomas / Halkjasr, Barbara / Svendsen, lb / Ottesen, Martin -- Pepstatin-sensitive proteinase from Chlamydomonas reinhardtii cells / Wilusz, T. / Polanowski, A. / Jones, R.F. / Jones, Raymond F. -- Purification and characterization of aspartic proteinases from Cucumis sativus and Cucurbita maxima seeds / Polanowski, Antoni / Wilusz, Tadeusz / Kołaczkowska, Maria K. / Wieczorek, Maciej / Wilimowska-Pelc, Anna / Kuczek, Marian -- Isolation and molecular characteristics of avian pepsins / Kostka, Vladimír / Pichová, Iva / Baudyš, Miroslav -- Pepsins of yak and camel. Isolation and characterization / Tomášek, Vladimír / Pohl, Jan / Kostka, Vladimír / Can-Erdene, Tudevin / Parevsuren, Badra / Dorzhpalam, Banzaryn -- Molecular variants of human aspartic proteinases / Samloff, I. Michael / Taggart, R. Thomas / Hengels, Klaus J. -- Human pepsins 1 and 2 ("fast pepsins"): Heterogeneity and carbohydrate content / Ryle, Andrew P. / Foltmann, Bent -- The primary structure of cathepsin D and the implications for its biological functions / Shewale, Jaiprakash G. / Takahashi, Takayuki / Tang, Jordan -- Some unexpected properties of cathepsin D / Wiederanders, Bernd / Kirschke, Heidrun / Schaper, Susanne / Valler, Martin J. / Kay, John -- New characteristics of a high molecular weight aspartic proteinase from bovine brain / Azaryan, Anahit / Barkhudaryan, Nina / Galoyan, Armen / Wiederanders, Bernd -- Isolation and properties of an aspartic proteinase from pig intestinal mucosa / Antonov, V.K. / Zilberman, M.I. / Vorotyntseva, T.I. -- Three-dimensional structures, hydrolytic mechanism and specificity -- X-ray diffraction analysis of porcine pepsin structure / Andreeva, N. / Zdanov, A. / Gustchina, A. / Fedorov, A. -- The high resolution structure of endothiapepsin / Blundell, Tom / Jenkins, John / Pearl, Laurence / Sewell, Trevor / Pedersen, Vibeke -- X-ray diffraction studies on penicillopepsin and its complexes: the hydrolytic mechanism / James, Michael N.G. / Sielecki, Anita R. / Hofmann, Theo -- Structure of the active site of pepsin and its complexes with inhibitors / Gustchina, Alla / Andreeva, Natalia -- The determination of the three-dimensional structure of chymosin / Safro, Mark / Andreeva, Nataliya / Zdanov, Alexander -- The extended binding cleft of aspartic proteinases and its role in peptide hydrolysis / Pearl, Laurence -- Zymogens of aspartic proteinases. Structure predictions from amino acid sequences -- Chemical approaches to the mechanism of aspartic proteinases / Antonov, Vladimir K. -- Interaction of aspartic proteinases with a new series of synthetic substrates and with inhibitors based on the propart of porcine pepsinogen / Dunn, Ben M. / Parten, Benne / Jimenez, Melba / Rolph, Carole E. / Valler, Martin / Kay, John -- Kinetic and fluorescence studies on chicken pepsin. The use of Cys 115 as the active site probe / Pohl, Jan / Štrop, Petr / Pichová, Iva / Bláha, Ivo / Kostka, Vladimír -- Zymogen activation pathways -- Multiplicity and intermediates of the activation mechanism of zymogens of gastric aspartic proteinases / Takahashi, Kenji / Kageyama, Takashi -- Cathepsins d and e: molecular characteristics and mechanism of activation / Turk, Vito / Lah, Tamara / Puizdar, Vida / Babnik, Joža / Kotnik, Matjaž / Kregar, Igor / Pain, Roger H. -- Activation of chicken pepsinogen and chicken pepsin propart peptide (p1 -p42) complex / Pichová, Iva / Pohl, Jan / Štrop, Petr / Kostka, Vladimír -- Chicken pepsin - activation peptide (p1 -p42) complex isolated and artificially formed: a comparison / Baudyš, Miroslav / Pichová, Iva / Pohl, Jan / Kostka, Vladimír -- Renin -- Renin and general aspartyl proteases: differences and similarities in structure and function / Inagami, Tadashi / Misono, Kunio / Chang, J.-J. / Takii, Yukio / Dykes, Colin -- Computer graphics modelling and the subsite specificities of human and mouse renins / Sibanda, B.L. / Hemmings, A.M. / Blundell, T.L. -- Changes of different forms of active and inactive renin under stress in rats / Jindra, Antonín / Kvetnănský, Richard -- Mouse renin gene structure, evolution and function / Burt, D.W. / Beecroft, L.J. / Mullins, J.J. / Pioli, D. / George, H. / Brooks, J. / Walker, J. / Brammar, W.J. -- Pepstatin insensitive acid proteinases / Murao, Sawao / Oda, Kohei -- Inhibitors of aspartic proteinases -- Renin inhibitors. design of angiotensin transition-state analogs containing statine / Boger, Joshua -- Chemistry of renin inhibitors / Szelke, Michael -- Human renin inhibitors / Leckie, B.J. -- Protection groups increase the in vivo stability of a statine-containing renin inhibitor / Wood, Jeanette M. / Fuhrer, Walter / Bühlmayer, Peter / Riniker, Bernhard / Hofbauer, Karl G. -- Inhibition of aspartic proteinases by transition state substrate analogs. X-ray studies of the complex of endothiapepsin with the renin inhibitor H-142 / Hallett, A. / Jones, D.M. / Atrash, B. / Szelke, M. / Leckie, B.J. / Beattie, S. / Dunn, B.M. / Valler, M.J. / Rolph, C.E. / Kay, J. / Foundling, S.I. / Wood, S.P. / Pearl, L.H. / Watson, F.E. / Blundell, T.L. -- Design and synthesis of statine-containing inhibitors of chymosin / Powell, M.J. / Holdworth, R.J. / Baker, T.S. / Titmas, R.C. / Bose, C.C. / Phipps, A. / Eaton, M. / Rolph, C.E. / Valler, M.J. / Kay, J. -- Interaction of cathepsin D and pepsin with alphaj-macroglobulin / Lah, Tamara / Vihar, Maja / Turk, Vito -- Analytical methods -- Methods for detection of proteinases: electrophoretic and immunological comparison of aspartic proteinases of different origins / Foltmann, Bent / Tarasova, Nadezhda I. / Szecsi, Pal B. -- Apparent inhibition of pepsin by an excess of haemoglobin substrate / Símonarson, Baldur -- Determination of chymosin by rocket Immunoelectrophoresis / Kleine, Rolf -- Occurrence and role of aspartic proteinases in biological systems -- Aspartic proteinases in gastric carcinomas / Reid, William A. / Valler, Martin J. / Kay, John -- Gastric proteinases in various diseases / Kučerová, Zdena / Korbová, Libuše / Čížková, Jiřina / Kohout, Jiří / Marek, Josef -- Activities of some proteolytic enzymes in the cartilage and subchondral bone of osteoarthrotic rabbits / Rohožková, D. / Tesárek, B. / Trnavský, K. -- Biotechnology aspects of aspartic proteinases -- Commercial aspects of aspartic proteases / Harboe, Marianne K. -- mRNA's for chymosin and pepsin, two main aspartic proteinases of bovine stomach and analysis of their translation products / Lipoldová, Marie / Čeřni, Jiřina / Takcáč, Mirko / Zadražil, Stanislav / Rychlík, Ivan -- Proteolytic degradation of muscle during the salt-curing process of herring / Ȯlafsdóttir, Sigríǒur / Magnússon, Sigurǒur / Bjarnason, Jón B. -- List of participants -- Author index -- Abbreviations -- Subject index
restricted access http://purl.org/coar/access_right/c_16ec online access with authorization star
Mode of access: Internet via World Wide Web.
In German.
Description based on online resource; title from PDF title page (publisher's Web site, viewed 21. Dez 2019)
Asparaginsäure-Proteinasen.
Asparaginsäureproteinase.
MEDICAL / Laboratory Medicine. bisacsh
Federation of European Biochemical Societies, , editor. edt http://id.loc.gov/vocabulary/relators/edt.
Kostka, Vladimír, editor. edt http://id.loc.gov/vocabulary/relators/edt.
Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences - <1990 9783110637861 ZDB-23-GML
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Federation of European Biochemical Societies, ,
Kostka, Vladimír,
Kostka, Vladimír,
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Federation of European Biochemical Societies, ,
Kostka, Vladimír,
Kostka, Vladimír,
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author2_role HerausgeberIn
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author_sort Federation of European Biochemical Societies, ,
author_additional Kay, John --
Foltmann, Bent --
Stepanov, Valentin M. --
Dreyer, Thomas / Halkjasr, Barbara / Svendsen, lb / Ottesen, Martin --
Wilusz, T. / Polanowski, A. / Jones, R.F. / Jones, Raymond F. --
Polanowski, Antoni / Wilusz, Tadeusz / Kołaczkowska, Maria K. / Wieczorek, Maciej / Wilimowska-Pelc, Anna / Kuczek, Marian --
Kostka, Vladimír / Pichová, Iva / Baudyš, Miroslav --
Tomášek, Vladimír / Pohl, Jan / Kostka, Vladimír / Can-Erdene, Tudevin / Parevsuren, Badra / Dorzhpalam, Banzaryn --
Samloff, I. Michael / Taggart, R. Thomas / Hengels, Klaus J. --
Ryle, Andrew P. / Foltmann, Bent --
Shewale, Jaiprakash G. / Takahashi, Takayuki / Tang, Jordan --
Wiederanders, Bernd / Kirschke, Heidrun / Schaper, Susanne / Valler, Martin J. / Kay, John --
Azaryan, Anahit / Barkhudaryan, Nina / Galoyan, Armen / Wiederanders, Bernd --
Antonov, V.K. / Zilberman, M.I. / Vorotyntseva, T.I. --
Andreeva, N. / Zdanov, A. / Gustchina, A. / Fedorov, A. --
Blundell, Tom / Jenkins, John / Pearl, Laurence / Sewell, Trevor / Pedersen, Vibeke --
James, Michael N.G. / Sielecki, Anita R. / Hofmann, Theo --
Gustchina, Alla / Andreeva, Natalia --
Safro, Mark / Andreeva, Nataliya / Zdanov, Alexander --
Pearl, Laurence --
Antonov, Vladimir K. --
Dunn, Ben M. / Parten, Benne / Jimenez, Melba / Rolph, Carole E. / Valler, Martin / Kay, John --
Pohl, Jan / Štrop, Petr / Pichová, Iva / Bláha, Ivo / Kostka, Vladimír --
Takahashi, Kenji / Kageyama, Takashi --
Turk, Vito / Lah, Tamara / Puizdar, Vida / Babnik, Joža / Kotnik, Matjaž / Kregar, Igor / Pain, Roger H. --
Pichová, Iva / Pohl, Jan / Štrop, Petr / Kostka, Vladimír --
Baudyš, Miroslav / Pichová, Iva / Pohl, Jan / Kostka, Vladimír --
Inagami, Tadashi / Misono, Kunio / Chang, J.-J. / Takii, Yukio / Dykes, Colin --
Sibanda, B.L. / Hemmings, A.M. / Blundell, T.L. --
Jindra, Antonín / Kvetnănský, Richard --
Burt, D.W. / Beecroft, L.J. / Mullins, J.J. / Pioli, D. / George, H. / Brooks, J. / Walker, J. / Brammar, W.J. --
Murao, Sawao / Oda, Kohei --
Boger, Joshua --
Szelke, Michael --
Leckie, B.J. --
Wood, Jeanette M. / Fuhrer, Walter / Bühlmayer, Peter / Riniker, Bernhard / Hofbauer, Karl G. --
Hallett, A. / Jones, D.M. / Atrash, B. / Szelke, M. / Leckie, B.J. / Beattie, S. / Dunn, B.M. / Valler, M.J. / Rolph, C.E. / Kay, J. / Foundling, S.I. / Wood, S.P. / Pearl, L.H. / Watson, F.E. / Blundell, T.L. --
Powell, M.J. / Holdworth, R.J. / Baker, T.S. / Titmas, R.C. / Bose, C.C. / Phipps, A. / Eaton, M. / Rolph, C.E. / Valler, M.J. / Kay, J. --
Lah, Tamara / Vihar, Maja / Turk, Vito --
Foltmann, Bent / Tarasova, Nadezhda I. / Szecsi, Pal B. --
Símonarson, Baldur --
Kleine, Rolf --
Reid, William A. / Valler, Martin J. / Kay, John --
Kučerová, Zdena / Korbová, Libuše / Čížková, Jiřina / Kohout, Jiří / Marek, Josef --
Rohožková, D. / Tesárek, B. / Trnavský, K. --
Harboe, Marianne K. --
Lipoldová, Marie / Čeřni, Jiřina / Takcáč, Mirko / Zadražil, Stanislav / Rychlík, Ivan --
Ȯlafsdóttir, Sigríǒur / Magnússon, Sigurǒur / Bjarnason, Jón B. --
title Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 /
spellingShingle Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 /
Frontmatter --
Preface --
Acknowledgements --
Organizing Committee --
Contents --
Introduction --
Aspartic proteinases and their inhibitors /
Comments on the nomenclature of aspartic proteinases /
General aspartic proteinases --
Isolation, molecufer characteristics, and primary structures. Fungal aspartyl proteinases /
Structure and properties of proteinase a from Saccharomyces carlsbergensis and Saccharomyces cerevisiae /
Pepstatin-sensitive proteinase from Chlamydomonas reinhardtii cells /
Purification and characterization of aspartic proteinases from Cucumis sativus and Cucurbita maxima seeds /
Isolation and molecular characteristics of avian pepsins /
Pepsins of yak and camel. Isolation and characterization /
Molecular variants of human aspartic proteinases /
Human pepsins 1 and 2 ("fast pepsins"): Heterogeneity and carbohydrate content /
The primary structure of cathepsin D and the implications for its biological functions /
Some unexpected properties of cathepsin D /
New characteristics of a high molecular weight aspartic proteinase from bovine brain /
Isolation and properties of an aspartic proteinase from pig intestinal mucosa /
Three-dimensional structures, hydrolytic mechanism and specificity --
X-ray diffraction analysis of porcine pepsin structure /
The high resolution structure of endothiapepsin /
X-ray diffraction studies on penicillopepsin and its complexes: the hydrolytic mechanism /
Structure of the active site of pepsin and its complexes with inhibitors /
The determination of the three-dimensional structure of chymosin /
The extended binding cleft of aspartic proteinases and its role in peptide hydrolysis /
Zymogens of aspartic proteinases. Structure predictions from amino acid sequences --
Chemical approaches to the mechanism of aspartic proteinases /
Interaction of aspartic proteinases with a new series of synthetic substrates and with inhibitors based on the propart of porcine pepsinogen /
Kinetic and fluorescence studies on chicken pepsin. The use of Cys 115 as the active site probe /
Zymogen activation pathways --
Multiplicity and intermediates of the activation mechanism of zymogens of gastric aspartic proteinases /
Cathepsins d and e: molecular characteristics and mechanism of activation /
Activation of chicken pepsinogen and chicken pepsin propart peptide (p1 -p42) complex /
Chicken pepsin - activation peptide (p1 -p42) complex isolated and artificially formed: a comparison /
Renin --
Renin and general aspartyl proteases: differences and similarities in structure and function /
Computer graphics modelling and the subsite specificities of human and mouse renins /
Changes of different forms of active and inactive renin under stress in rats /
Mouse renin gene structure, evolution and function /
Pepstatin insensitive acid proteinases /
Inhibitors of aspartic proteinases --
Renin inhibitors. design of angiotensin transition-state analogs containing statine /
Chemistry of renin inhibitors /
Human renin inhibitors /
Protection groups increase the in vivo stability of a statine-containing renin inhibitor /
Inhibition of aspartic proteinases by transition state substrate analogs. X-ray studies of the complex of endothiapepsin with the renin inhibitor H-142 /
Design and synthesis of statine-containing inhibitors of chymosin /
Interaction of cathepsin D and pepsin with alphaj-macroglobulin /
Analytical methods --
Methods for detection of proteinases: electrophoretic and immunological comparison of aspartic proteinases of different origins /
Apparent inhibition of pepsin by an excess of haemoglobin substrate /
Determination of chymosin by rocket Immunoelectrophoresis /
Occurrence and role of aspartic proteinases in biological systems --
Aspartic proteinases in gastric carcinomas /
Gastric proteinases in various diseases /
Activities of some proteolytic enzymes in the cartilage and subchondral bone of osteoarthrotic rabbits /
Biotechnology aspects of aspartic proteinases --
Commercial aspects of aspartic proteases /
mRNA's for chymosin and pepsin, two main aspartic proteinases of bovine stomach and analysis of their translation products /
Proteolytic degradation of muscle during the salt-curing process of herring /
List of participants --
Author index --
Abbreviations --
Subject index
title_sub Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 /
title_full Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 / Vladimír Kostka, Federation of European Biochemical Societies.
title_fullStr Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 / Vladimír Kostka, Federation of European Biochemical Societies.
title_full_unstemmed Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 / Vladimír Kostka, Federation of European Biochemical Societies.
title_auth Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 /
title_alt Frontmatter --
Preface --
Acknowledgements --
Organizing Committee --
Contents --
Introduction --
Aspartic proteinases and their inhibitors /
Comments on the nomenclature of aspartic proteinases /
General aspartic proteinases --
Isolation, molecufer characteristics, and primary structures. Fungal aspartyl proteinases /
Structure and properties of proteinase a from Saccharomyces carlsbergensis and Saccharomyces cerevisiae /
Pepstatin-sensitive proteinase from Chlamydomonas reinhardtii cells /
Purification and characterization of aspartic proteinases from Cucumis sativus and Cucurbita maxima seeds /
Isolation and molecular characteristics of avian pepsins /
Pepsins of yak and camel. Isolation and characterization /
Molecular variants of human aspartic proteinases /
Human pepsins 1 and 2 ("fast pepsins"): Heterogeneity and carbohydrate content /
The primary structure of cathepsin D and the implications for its biological functions /
Some unexpected properties of cathepsin D /
New characteristics of a high molecular weight aspartic proteinase from bovine brain /
Isolation and properties of an aspartic proteinase from pig intestinal mucosa /
Three-dimensional structures, hydrolytic mechanism and specificity --
X-ray diffraction analysis of porcine pepsin structure /
The high resolution structure of endothiapepsin /
X-ray diffraction studies on penicillopepsin and its complexes: the hydrolytic mechanism /
Structure of the active site of pepsin and its complexes with inhibitors /
The determination of the three-dimensional structure of chymosin /
The extended binding cleft of aspartic proteinases and its role in peptide hydrolysis /
Zymogens of aspartic proteinases. Structure predictions from amino acid sequences --
Chemical approaches to the mechanism of aspartic proteinases /
Interaction of aspartic proteinases with a new series of synthetic substrates and with inhibitors based on the propart of porcine pepsinogen /
Kinetic and fluorescence studies on chicken pepsin. The use of Cys 115 as the active site probe /
Zymogen activation pathways --
Multiplicity and intermediates of the activation mechanism of zymogens of gastric aspartic proteinases /
Cathepsins d and e: molecular characteristics and mechanism of activation /
Activation of chicken pepsinogen and chicken pepsin propart peptide (p1 -p42) complex /
Chicken pepsin - activation peptide (p1 -p42) complex isolated and artificially formed: a comparison /
Renin --
Renin and general aspartyl proteases: differences and similarities in structure and function /
Computer graphics modelling and the subsite specificities of human and mouse renins /
Changes of different forms of active and inactive renin under stress in rats /
Mouse renin gene structure, evolution and function /
Pepstatin insensitive acid proteinases /
Inhibitors of aspartic proteinases --
Renin inhibitors. design of angiotensin transition-state analogs containing statine /
Chemistry of renin inhibitors /
Human renin inhibitors /
Protection groups increase the in vivo stability of a statine-containing renin inhibitor /
Inhibition of aspartic proteinases by transition state substrate analogs. X-ray studies of the complex of endothiapepsin with the renin inhibitor H-142 /
Design and synthesis of statine-containing inhibitors of chymosin /
Interaction of cathepsin D and pepsin with alphaj-macroglobulin /
Analytical methods --
Methods for detection of proteinases: electrophoretic and immunological comparison of aspartic proteinases of different origins /
Apparent inhibition of pepsin by an excess of haemoglobin substrate /
Determination of chymosin by rocket Immunoelectrophoresis /
Occurrence and role of aspartic proteinases in biological systems --
Aspartic proteinases in gastric carcinomas /
Gastric proteinases in various diseases /
Activities of some proteolytic enzymes in the cartilage and subchondral bone of osteoarthrotic rabbits /
Biotechnology aspects of aspartic proteinases --
Commercial aspects of aspartic proteases /
mRNA's for chymosin and pepsin, two main aspartic proteinases of bovine stomach and analysis of their translation products /
Proteolytic degradation of muscle during the salt-curing process of herring /
List of participants --
Author index --
Abbreviations --
Subject index
title_new Aspartic Proteinases and Their Inhibitors :
title_sort aspartic proteinases and their inhibitors : proceedings of the febs advanced course no. 84/07, prague, czechoslovakia, august 20-24, 1984 /
publisher De Gruyter,
publishDate 2016
physical 1 online resource (613 p.) : Zahlr. Abb.
edition Reprint 2015
contents Frontmatter --
Preface --
Acknowledgements --
Organizing Committee --
Contents --
Introduction --
Aspartic proteinases and their inhibitors /
Comments on the nomenclature of aspartic proteinases /
General aspartic proteinases --
Isolation, molecufer characteristics, and primary structures. Fungal aspartyl proteinases /
Structure and properties of proteinase a from Saccharomyces carlsbergensis and Saccharomyces cerevisiae /
Pepstatin-sensitive proteinase from Chlamydomonas reinhardtii cells /
Purification and characterization of aspartic proteinases from Cucumis sativus and Cucurbita maxima seeds /
Isolation and molecular characteristics of avian pepsins /
Pepsins of yak and camel. Isolation and characterization /
Molecular variants of human aspartic proteinases /
Human pepsins 1 and 2 ("fast pepsins"): Heterogeneity and carbohydrate content /
The primary structure of cathepsin D and the implications for its biological functions /
Some unexpected properties of cathepsin D /
New characteristics of a high molecular weight aspartic proteinase from bovine brain /
Isolation and properties of an aspartic proteinase from pig intestinal mucosa /
Three-dimensional structures, hydrolytic mechanism and specificity --
X-ray diffraction analysis of porcine pepsin structure /
The high resolution structure of endothiapepsin /
X-ray diffraction studies on penicillopepsin and its complexes: the hydrolytic mechanism /
Structure of the active site of pepsin and its complexes with inhibitors /
The determination of the three-dimensional structure of chymosin /
The extended binding cleft of aspartic proteinases and its role in peptide hydrolysis /
Zymogens of aspartic proteinases. Structure predictions from amino acid sequences --
Chemical approaches to the mechanism of aspartic proteinases /
Interaction of aspartic proteinases with a new series of synthetic substrates and with inhibitors based on the propart of porcine pepsinogen /
Kinetic and fluorescence studies on chicken pepsin. The use of Cys 115 as the active site probe /
Zymogen activation pathways --
Multiplicity and intermediates of the activation mechanism of zymogens of gastric aspartic proteinases /
Cathepsins d and e: molecular characteristics and mechanism of activation /
Activation of chicken pepsinogen and chicken pepsin propart peptide (p1 -p42) complex /
Chicken pepsin - activation peptide (p1 -p42) complex isolated and artificially formed: a comparison /
Renin --
Renin and general aspartyl proteases: differences and similarities in structure and function /
Computer graphics modelling and the subsite specificities of human and mouse renins /
Changes of different forms of active and inactive renin under stress in rats /
Mouse renin gene structure, evolution and function /
Pepstatin insensitive acid proteinases /
Inhibitors of aspartic proteinases --
Renin inhibitors. design of angiotensin transition-state analogs containing statine /
Chemistry of renin inhibitors /
Human renin inhibitors /
Protection groups increase the in vivo stability of a statine-containing renin inhibitor /
Inhibition of aspartic proteinases by transition state substrate analogs. X-ray studies of the complex of endothiapepsin with the renin inhibitor H-142 /
Design and synthesis of statine-containing inhibitors of chymosin /
Interaction of cathepsin D and pepsin with alphaj-macroglobulin /
Analytical methods --
Methods for detection of proteinases: electrophoretic and immunological comparison of aspartic proteinases of different origins /
Apparent inhibition of pepsin by an excess of haemoglobin substrate /
Determination of chymosin by rocket Immunoelectrophoresis /
Occurrence and role of aspartic proteinases in biological systems --
Aspartic proteinases in gastric carcinomas /
Gastric proteinases in various diseases /
Activities of some proteolytic enzymes in the cartilage and subchondral bone of osteoarthrotic rabbits /
Biotechnology aspects of aspartic proteinases --
Commercial aspects of aspartic proteases /
mRNA's for chymosin and pepsin, two main aspartic proteinases of bovine stomach and analysis of their translation products /
Proteolytic degradation of muscle during the salt-curing process of herring /
List of participants --
Author index --
Abbreviations --
Subject index
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fullrecord <?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>09932nam a22006255i 4500</leader><controlfield tag="001">9783111649788</controlfield><controlfield tag="003">DE-B1597</controlfield><controlfield tag="005">20191221113333.0</controlfield><controlfield tag="006">m|||||o||d||||||||</controlfield><controlfield tag="007">cr || ||||||||</controlfield><controlfield tag="008">191221s2016 gw fo d z ger d</controlfield><datafield tag="020" ind1=" " ind2=" "><subfield code="a">9783111649788</subfield></datafield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1515/9783111649788</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-B1597)96737</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(OCoLC)979631599</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-B1597</subfield><subfield code="b">eng</subfield><subfield code="c">DE-B1597</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1="0" ind2=" "><subfield code="a">ger</subfield></datafield><datafield tag="044" ind1=" " ind2=" "><subfield code="a">gw</subfield><subfield code="c">DE</subfield></datafield><datafield tag="072" ind1=" " ind2="7"><subfield code="a">MED047000</subfield><subfield code="2">bisacsh</subfield></datafield><datafield tag="245" ind1="0" ind2="0"><subfield code="a">Aspartic Proteinases and Their Inhibitors :</subfield><subfield code="b">Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20-24, 1984 /</subfield><subfield code="c">Vladimír Kostka, Federation of European Biochemical Societies.</subfield></datafield><datafield tag="250" ind1=" " ind2=" "><subfield code="a">Reprint 2015</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Berlin ;</subfield><subfield code="a">Boston : </subfield><subfield code="b">De Gruyter, </subfield><subfield code="c">[2016]</subfield></datafield><datafield tag="264" ind1=" " ind2="4"><subfield code="c">©1985</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">1 online resource (613 p.) :</subfield><subfield code="b">Zahlr. Abb.</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">computer</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">online resource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="347" ind1=" " ind2=" "><subfield code="a">text file</subfield><subfield code="b">PDF</subfield><subfield code="2">rda</subfield></datafield><datafield tag="505" ind1="0" ind2="0"><subfield code="t">Frontmatter -- </subfield><subfield code="t">Preface -- </subfield><subfield code="t">Acknowledgements -- </subfield><subfield code="t">Organizing Committee -- </subfield><subfield code="t">Contents -- </subfield><subfield code="t">Introduction -- </subfield><subfield code="t">Aspartic proteinases and their inhibitors / </subfield><subfield code="r">Kay, John -- </subfield><subfield code="t">Comments on the nomenclature of aspartic proteinases / </subfield><subfield code="r">Foltmann, Bent -- </subfield><subfield code="t">General aspartic proteinases -- </subfield><subfield code="t">Isolation, molecufer characteristics, and primary structures. Fungal aspartyl proteinases / </subfield><subfield code="r">Stepanov, Valentin M. -- </subfield><subfield code="t">Structure and properties of proteinase a from Saccharomyces carlsbergensis and Saccharomyces cerevisiae / </subfield><subfield code="r">Dreyer, Thomas / Halkjasr, Barbara / Svendsen, lb / Ottesen, Martin -- </subfield><subfield code="t">Pepstatin-sensitive proteinase from Chlamydomonas reinhardtii cells / </subfield><subfield code="r">Wilusz, T. / Polanowski, A. / Jones, R.F. / Jones, Raymond F. -- </subfield><subfield code="t">Purification and characterization of aspartic proteinases from Cucumis sativus and Cucurbita maxima seeds / </subfield><subfield code="r">Polanowski, Antoni / Wilusz, Tadeusz / Kołaczkowska, Maria K. / Wieczorek, Maciej / Wilimowska-Pelc, Anna / Kuczek, Marian -- </subfield><subfield code="t">Isolation and molecular characteristics of avian pepsins / </subfield><subfield code="r">Kostka, Vladimír / Pichová, Iva / Baudyš, Miroslav -- </subfield><subfield code="t">Pepsins of yak and camel. Isolation and characterization / </subfield><subfield code="r">Tomášek, Vladimír / Pohl, Jan / Kostka, Vladimír / Can-Erdene, Tudevin / Parevsuren, Badra / Dorzhpalam, Banzaryn -- </subfield><subfield code="t">Molecular variants of human aspartic proteinases / </subfield><subfield code="r">Samloff, I. Michael / Taggart, R. Thomas / Hengels, Klaus J. -- </subfield><subfield code="t">Human pepsins 1 and 2 ("fast pepsins"): Heterogeneity and carbohydrate content / </subfield><subfield code="r">Ryle, Andrew P. / Foltmann, Bent -- </subfield><subfield code="t">The primary structure of cathepsin D and the implications for its biological functions / </subfield><subfield code="r">Shewale, Jaiprakash G. / Takahashi, Takayuki / Tang, Jordan -- </subfield><subfield code="t">Some unexpected properties of cathepsin D / </subfield><subfield code="r">Wiederanders, Bernd / Kirschke, Heidrun / Schaper, Susanne / Valler, Martin J. / Kay, John -- </subfield><subfield code="t">New characteristics of a high molecular weight aspartic proteinase from bovine brain / </subfield><subfield code="r">Azaryan, Anahit / Barkhudaryan, Nina / Galoyan, Armen / Wiederanders, Bernd -- </subfield><subfield code="t">Isolation and properties of an aspartic proteinase from pig intestinal mucosa / </subfield><subfield code="r">Antonov, V.K. / Zilberman, M.I. / Vorotyntseva, T.I. -- </subfield><subfield code="t">Three-dimensional structures, hydrolytic mechanism and specificity -- </subfield><subfield code="t">X-ray diffraction analysis of porcine pepsin structure / </subfield><subfield code="r">Andreeva, N. / Zdanov, A. / Gustchina, A. / Fedorov, A. -- </subfield><subfield code="t">The high resolution structure of endothiapepsin / </subfield><subfield code="r">Blundell, Tom / Jenkins, John / Pearl, Laurence / Sewell, Trevor / Pedersen, Vibeke -- </subfield><subfield code="t">X-ray diffraction studies on penicillopepsin and its complexes: the hydrolytic mechanism / </subfield><subfield code="r">James, Michael N.G. / Sielecki, Anita R. / Hofmann, Theo -- </subfield><subfield code="t">Structure of the active site of pepsin and its complexes with inhibitors / </subfield><subfield code="r">Gustchina, Alla / Andreeva, Natalia -- </subfield><subfield code="t">The determination of the three-dimensional structure of chymosin / </subfield><subfield code="r">Safro, Mark / Andreeva, Nataliya / Zdanov, Alexander -- </subfield><subfield code="t">The extended binding cleft of aspartic proteinases and its role in peptide hydrolysis / </subfield><subfield code="r">Pearl, Laurence -- </subfield><subfield code="t">Zymogens of aspartic proteinases. Structure predictions from amino acid sequences -- </subfield><subfield code="t">Chemical approaches to the mechanism of aspartic proteinases / </subfield><subfield code="r">Antonov, Vladimir K. -- </subfield><subfield code="t">Interaction of aspartic proteinases with a new series of synthetic substrates and with inhibitors based on the propart of porcine pepsinogen / </subfield><subfield code="r">Dunn, Ben M. / Parten, Benne / Jimenez, Melba / Rolph, Carole E. / Valler, Martin / Kay, John -- </subfield><subfield code="t">Kinetic and fluorescence studies on chicken pepsin. The use of Cys 115 as the active site probe / </subfield><subfield code="r">Pohl, Jan / Štrop, Petr / Pichová, Iva / Bláha, Ivo / Kostka, Vladimír -- </subfield><subfield code="t">Zymogen activation pathways -- </subfield><subfield code="t">Multiplicity and intermediates of the activation mechanism of zymogens of gastric aspartic proteinases / </subfield><subfield code="r">Takahashi, Kenji / Kageyama, Takashi -- </subfield><subfield code="t">Cathepsins d and e: molecular characteristics and mechanism of activation / </subfield><subfield code="r">Turk, Vito / Lah, Tamara / Puizdar, Vida / Babnik, Joža / Kotnik, Matjaž / Kregar, Igor / Pain, Roger H. -- </subfield><subfield code="t">Activation of chicken pepsinogen and chicken pepsin propart peptide (p1 -p42) complex / </subfield><subfield code="r">Pichová, Iva / Pohl, Jan / Štrop, Petr / Kostka, Vladimír -- </subfield><subfield code="t">Chicken pepsin - activation peptide (p1 -p42) complex isolated and artificially formed: a comparison / </subfield><subfield code="r">Baudyš, Miroslav / Pichová, Iva / Pohl, Jan / Kostka, Vladimír -- </subfield><subfield code="t">Renin -- </subfield><subfield code="t">Renin and general aspartyl proteases: differences and similarities in structure and function / </subfield><subfield code="r">Inagami, Tadashi / Misono, Kunio / Chang, J.-J. / Takii, Yukio / Dykes, Colin -- </subfield><subfield code="t">Computer graphics modelling and the subsite specificities of human and mouse renins / </subfield><subfield code="r">Sibanda, B.L. / Hemmings, A.M. / Blundell, T.L. -- </subfield><subfield code="t">Changes of different forms of active and inactive renin under stress in rats / </subfield><subfield code="r">Jindra, Antonín / Kvetnănský, Richard -- </subfield><subfield code="t">Mouse renin gene structure, evolution and function / </subfield><subfield code="r">Burt, D.W. / Beecroft, L.J. / Mullins, J.J. / Pioli, D. / George, H. / Brooks, J. / Walker, J. / Brammar, W.J. -- </subfield><subfield code="t">Pepstatin insensitive acid proteinases / </subfield><subfield code="r">Murao, Sawao / Oda, Kohei -- </subfield><subfield code="t">Inhibitors of aspartic proteinases -- </subfield><subfield code="t">Renin inhibitors. design of angiotensin transition-state analogs containing statine / </subfield><subfield code="r">Boger, Joshua -- </subfield><subfield code="t">Chemistry of renin inhibitors / </subfield><subfield code="r">Szelke, Michael -- </subfield><subfield code="t">Human renin inhibitors / </subfield><subfield code="r">Leckie, B.J. -- </subfield><subfield code="t">Protection groups increase the in vivo stability of a statine-containing renin inhibitor / </subfield><subfield code="r">Wood, Jeanette M. / Fuhrer, Walter / Bühlmayer, Peter / Riniker, Bernhard / Hofbauer, Karl G. -- </subfield><subfield code="t">Inhibition of aspartic proteinases by transition state substrate analogs. X-ray studies of the complex of endothiapepsin with the renin inhibitor H-142 / </subfield><subfield code="r">Hallett, A. / Jones, D.M. / Atrash, B. / Szelke, M. / Leckie, B.J. / Beattie, S. / Dunn, B.M. / Valler, M.J. / Rolph, C.E. / Kay, J. / Foundling, S.I. / Wood, S.P. / Pearl, L.H. / Watson, F.E. / Blundell, T.L. -- </subfield><subfield code="t">Design and synthesis of statine-containing inhibitors of chymosin / </subfield><subfield code="r">Powell, M.J. / Holdworth, R.J. / Baker, T.S. / Titmas, R.C. / Bose, C.C. / Phipps, A. / Eaton, M. / Rolph, C.E. / Valler, M.J. / Kay, J. -- </subfield><subfield code="t">Interaction of cathepsin D and pepsin with alphaj-macroglobulin / </subfield><subfield code="r">Lah, Tamara / Vihar, Maja / Turk, Vito -- </subfield><subfield code="t">Analytical methods -- </subfield><subfield code="t">Methods for detection of proteinases: electrophoretic and immunological comparison of aspartic proteinases of different origins / </subfield><subfield code="r">Foltmann, Bent / Tarasova, Nadezhda I. / Szecsi, Pal B. -- </subfield><subfield code="t">Apparent inhibition of pepsin by an excess of haemoglobin substrate / </subfield><subfield code="r">Símonarson, Baldur -- </subfield><subfield code="t">Determination of chymosin by rocket Immunoelectrophoresis / </subfield><subfield code="r">Kleine, Rolf -- </subfield><subfield code="t">Occurrence and role of aspartic proteinases in biological systems -- </subfield><subfield code="t">Aspartic proteinases in gastric carcinomas / </subfield><subfield code="r">Reid, William A. / Valler, Martin J. / Kay, John -- </subfield><subfield code="t">Gastric proteinases in various diseases / </subfield><subfield code="r">Kučerová, Zdena / Korbová, Libuše / Čížková, Jiřina / Kohout, Jiří / Marek, Josef -- </subfield><subfield code="t">Activities of some proteolytic enzymes in the cartilage and subchondral bone of osteoarthrotic rabbits / </subfield><subfield code="r">Rohožková, D. / Tesárek, B. / Trnavský, K. -- </subfield><subfield code="t">Biotechnology aspects of aspartic proteinases -- </subfield><subfield code="t">Commercial aspects of aspartic proteases / </subfield><subfield code="r">Harboe, Marianne K. -- </subfield><subfield code="t">mRNA's for chymosin and pepsin, two main aspartic proteinases of bovine stomach and analysis of their translation products / </subfield><subfield code="r">Lipoldová, Marie / Čeřni, Jiřina / Takcáč, Mirko / Zadražil, Stanislav / Rychlík, Ivan -- </subfield><subfield code="t">Proteolytic degradation of muscle during the salt-curing process of herring / </subfield><subfield code="r">Ȯlafsdóttir, Sigríǒur / Magnússon, Sigurǒur / Bjarnason, Jón B. -- </subfield><subfield code="t">List of participants -- </subfield><subfield code="t">Author index -- </subfield><subfield code="t">Abbreviations -- </subfield><subfield code="t">Subject index</subfield></datafield><datafield tag="506" ind1="0" ind2=" "><subfield code="a">restricted access</subfield><subfield code="u">http://purl.org/coar/access_right/c_16ec</subfield><subfield code="f">online access with authorization</subfield><subfield code="2">star</subfield></datafield><datafield tag="538" ind1=" " ind2=" "><subfield code="a">Mode of access: Internet via World Wide Web.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">In German.</subfield></datafield><datafield tag="588" ind1="0" ind2=" "><subfield code="a">Description based on online resource; title from PDF title page (publisher's Web site, viewed 21. 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