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Titlebook: Aspartic Proteinases; Structure, Function, Kenji Takahashi Book 1995 The Editor(s) (if applicable) and The Author(s), under exclusive licen

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发表于 2025-3-21 20:09:35 | 显示全部楼层 |阅读模式
期刊全称Aspartic Proteinases
期刊简称Structure, Function,
影响因子2023Kenji Takahashi
视频video
学科分类Advances in Experimental Medicine and Biology
图书封面Titlebook: Aspartic Proteinases; Structure, Function, Kenji Takahashi Book 1995 The Editor(s) (if applicable) and The Author(s), under exclusive licen
影响因子The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima­ cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32 papers were presented by invited speakers, and 58 papers as posters. The purpose of this conference was to present and discuss new information on the structure, function, and biology, and related topics, including biomedical implications, of aspartic proteinases, and this book is a collec­ tion of nearly all the papers presented at the meeting. Aspartic proteinases belong to one of the four major classes of proteinases, the others being serine, cysteine, and metalloproteinases, and are so called since they have two catalytic aspartic acid residues in common in their active sites. Most of them are optimally active at acidic pH, hence the long-used name "acid proteinases," which, indeed, was the major title of the first conference of this series. However, some of them are active at around neutral pH, indicating their physiological roles in a wider range
Pindex Book 1995
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The Molecular Structure of Human Progastricsin and its Comparison with that of Porcine Pepsinogenocatalytically at pH < 5.0 (1). The human gastric juice has two major groups of aspartic proteinases, the pepsins (EC3.4.23.1) and the gastricsins (EC3.4.23.3). Progastricsin or pepsinogen C (PGC) is converted to gastricsin by removal of the 43 amino-terminal residues of the prosegment. The resultin
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Rearranging Pepsinogen and Pepsin by Protein Engineeringilobal structures. The three-dimensional structures of the N- and C-terminal lobes are homologous. It has been hypothesized that the origin of this internal similarity in eukaryotic aspartic proteases is derived from an evolutionary process of gene duplication and fusion (1). A primordial form of as
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Transcription Regulation of Human and Porcine Pepsinogen Ainical point of view pepsinogen gene regulation is interesting. Pepsinogen, activated by acid to pepsin, is one of the aggressive factors in the stomach that play a role in peptic ulcer disease (1). A dominantly inherited high pepsinogen A (PGA) output is associated with duodenal ulcer (2). On the o
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A Comparative Study on Amino Acid Sequences of Three Major Isoforms of Human Pepsin Ances has hindered progress to any clear explanation for these differences. The sequence data available has been based mainly on N-terminal amino-acid and cDNA analysis of human pepsinogens [2, 4, 5]. We have therefore undertaken further more detailed amino-acid sequence studies of isolated human pep
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Evidence for Electrostatic Interactions in the S2 Subsite of Porcine PepsinPepsin, a member of this family involved in the digestion of proteins in the stomach, has been a valuable model system for investigation into enzymatic specificity. The active site cleft of porcine pepsin is made of distinct subsites S.-S.’ (I. Schecter and A. Berger, 1967, B. B. R. C. .: 157) all o
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