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, Vladimír Kostka, Federation of European Biochemical Societies

• Verlag: De Gruyter
• Jahr: 2016
• ISBN drucken:
  9783111266329
• eBook-ISBN:
  9783111649788
• Thema: Medicine
• Thema: Medical Microbiology & Parasitology

Keine ausführliche Beschreibung für "Aspartic Proteinases and Their Inhibitors" verfügbar.

Inhaltsverzeichnis

• 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