WHY AND WHAT FOR IS PEPSIN STABLE AND ACTIVE AT PH 2

Authors
ANDREEVA NS
Citation
Ns. Andreeva, WHY AND WHAT FOR IS PEPSIN STABLE AND ACTIVE AT PH 2, Molecular biology, 28(6), 1994, pp. 869-873
Citations number
12
Categorie Soggetti
Biology
Journal title
Molecular biology → ACNP
ISSN journal
00268933
Volume
28
Issue
6
Year of publication
1994
Part
2
Pages
869 - 873
Database
ISI
SICI code
0026-8933(1994)28:6<869:WAWFIP>2.0.ZU;2-Y
Abstract
The results of recent studies can explain why despite the extreme cond itions (pH 1-2) the gastric epithelium remains intact, and the gastric proteinase pepsin [EC 3.4.32.1] is structurally stable and most activ e. The interpretation is based on detailed analysis of the disposition of masked charged groups in the enzyme 3D structure and on experiment s modeling the secretion of hydrochloric acid into the gastric lumen.