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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Superior document: | Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences - <1990 |
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Place / Publishing House: | Berlin ;, Boston : : De Gruyter, , [2016] ©1985 |
Year of Publication: | 2016 |
Edition: | Reprint 2015 |
Language: | German |
Online Access: | |
Physical Description: | 1 online resource (613 p.) :; Zahlr. Abb. |
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Other title: | 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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Format: | Mode of access: Internet via World Wide Web. |
ISBN: | 9783111649788 9783110637861 |
DOI: | 10.1515/9783111649788 |
Access: | restricted access |
Hierarchical level: | Monograph |
Statement of Responsibility: | Vladimír Kostka, Federation of European Biochemical Societies. |