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Indian J Biochem Biophys ; 1994 Apr; 31(2): 136-7
Article in English | IMSEAR | ID: sea-27418

ABSTRACT

The synthetic peptides AC-Glu-Phe-Phe (NO2)-Arg-amide (peptide VP) and AC-Ile-Glu-Phe-Phe (NO2)-Arg-amide (peptide VIP) are more readily hydrolyzed by human pepsin in gastric juice of patients of gastritis than those of duodenal ulcer and normal subjects. The kinetic parameters suggest that S3 subsite of the enzyme plays a role in the elevation of enzyme activity in gastric disease.


Subject(s)
Amino Acid Sequence , Binding Sites , Duodenal Ulcer/enzymology , Gastric Juice/enzymology , Gastritis/enzymology , Humans , Kinetics , Molecular Sequence Data , Oligopeptides/metabolism , Pepsin A/metabolism , Reference Values , Substrate Specificity , Vasoactive Intestinal Peptide/metabolism
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