Overview
- Editors:
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Jordan Tang
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Oklahoma Medical Research Foundation, USA
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Table of contents (20 chapters)
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Primary and Three-Dimensional Structures
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- Bent Foltmann, Vibeke Barkholt Pedersen
Pages 3-22
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- N. S. Andreeva, A. E. Gustchina, A. A. Fedorov, N. E. Shutzkever, T. V. Volnova
Pages 23-31
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- E. Subramanian, M. Liu, I. D. A. Swan, D. R. Davies
Pages 33-41
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- John Jenkins, Ian Tickle, Trevor Sewell, Luciano Ungaretti, Axel Wollmer, Tom Blundell
Pages 43-60
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- I-Nan Hsu, Louis T. J. Delbaere, Michael N. G. James, Theo Hofmann
Pages 61-81
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Mechanism of Pepsinogen Activation
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- Jean A. Hartsuck, Joseph Marciniszyn Jr., Jung San Huang, Jordan Tang
Pages 85-102
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Catalytic Mechanism of Pepsin
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Front Matter
Pages 129-129
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- James C. Powers, A. Dale Harley, Dirck V. Myers
Pages 141-157
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- E. T. Kaiser, Y. Nakagawa
Pages 159-177
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- Joseph Marciniszyn Jr., Jean A. Hartsuck, Jordan Tang
Pages 199-210
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- P. M. Harish Kumar, Peter H. Ward, Beatrice Kassell
Pages 211-222
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Acid Proteases in Various Biological Systems
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Front Matter
Pages 223-223
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- Tadashi Inagami, Kazuo Murakami, Kunio Misono, Robert J. Workman, Stanley Cohen, Yasunobu Suketa
Pages 225-247
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- B. J. Leckie, A. McConnell, J. Jordan
Pages 249-269
About this book
In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been pub lished. Their coverage of acid proteases has been limited, mainly due to the lack of significant new information on the structure of these enzymes. In the last four years, however, the primary and tertiary structures of a number of acid proteases have been deter mined, prompting the need to discuss the meanings of the old data and the possibilities for new experimentations. It was for this purpose that the "Conference on Acid Proteases: Structure, Function, and Biology" was organized. It took place at the University of Oklahoma on November 21-24, 1976. This book is a collection of the main lectures delivered at the Conference. Acid Proteases, by definition refers to a group of proteases having an optimal pH in acidic solutions. The classic examples are pepsin and chymosin. Some catalytic features are obviously shared by these proteases, most notably, their inhibition by pepstatin. The use of active center-directed inactivators such as diazoacetyl norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has shown that two catalytic aspartyl residues are present in most of these enzymes. These apparent cornmon features have prompted the suggestion by several investigators to name this group of enzymes "aspartyl proteases" or "carboxyl proteases".
Editors and Affiliations
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Oklahoma Medical Research Foundation, USA
Jordan Tang