Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is initiated by a peptic cleavage of the protein chain, a single enzymic site is formed. This site is made up, quite probably, of the secondary carboxyl group of glutamic acid or of aspartic acid and a tyrosine phenol group in close proximity so that they can form hydrogen or hydrophobic bonds with the substrate in some unique manner that permits hydrolysis to occur at an accelerated rate.
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1 March 1962
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March 01 1962
Pepsinogen and Pepsin
Roger M. Herriott
Roger M. Herriott
From the Department of Biochemistry, The Johns Hopkins University School of Hygiene and Public Health, Baltimore
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Roger M. Herriott
From the Department of Biochemistry, The Johns Hopkins University School of Hygiene and Public Health, Baltimore
Online ISSN: 1540-7748
Print ISSN: 0022-1295
Copyright, 1962, by The Rockefeller Institute Press.
1962
J Gen Physiol (1962) 45 (4): 57–76.
Citation
Roger M. Herriott; Pepsinogen and Pepsin . J Gen Physiol 1 March 1962; 45 (4): 57–76. doi: https://doi.org/10.1085/jgp.45.4.57
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