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.

• Superior document: Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences - <1990
• HerausgeberIn: Federation of European Biochemical Societies, ,
• Author: Kostka, Vladimír,
• Place / Publishing House: Berlin ;, Boston : : De Gruyter, , [2016]; ©1985
• Year of Publication: 2016
• Edition: Reprint 2015
• Language: German
• Physical Description: 1 online resource (613 p.) :; Zahlr. Abb.
• 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
• 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.