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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書目名稱Aspartic Proteinases影響因子(影響力)




書目名稱Aspartic Proteinases影響因子(影響力)學(xué)科排名




書目名稱Aspartic Proteinases網(wǎng)絡(luò)公開度




書目名稱Aspartic Proteinases網(wǎng)絡(luò)公開度學(xué)科排名




書目名稱Aspartic Proteinases被引頻次




書目名稱Aspartic Proteinases被引頻次學(xué)科排名




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書目名稱Aspartic Proteinases年度引用學(xué)科排名




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書目名稱Aspartic Proteinases讀者反饋學(xué)科排名

grandiose

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

foppish

希望

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

GREEN

AWL

迎合

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

苦惱

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

拖債

束以馬具

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