Aspartic Proteinases and Their Inhibitors : Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20–24, 1984

Die "Historische Kommission zu Berlin" betreibt die Erforschung der Landesgeschichte und der Historischen Landeskunde Berlin-Brandenburgs bzw. Brandenburg-Preußens in Form von wissenschaftlichen Untersuchungen, Vorträgen, Tagungen und Veröffentlichungen sowie durch Serviceleistungen. Dabei kooperiert die Kommission auch mit anderen Institutionen und begleitet wissenschaftliche und praktische Vorhaben von allgemeinem öffentlichen Interesse. In der Schriftenreihe werden die Ergebnisse der einzelnen wissenschaftlichen Projekte der Kommission veröffentlicht. 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