Aspartic Proteinases and Their Inhibitors

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