1. Subsite study of human pepsin in disease.
- Author
-
Balbaa M, Hamed EA, el-Ashwah A, Salem O, and Shamss-Eldin A
- Subjects
- Amino Acid Sequence, Binding Sites, Humans, Kinetics, Molecular Sequence Data, Reference Values, Substrate Specificity, Duodenal Ulcer enzymology, Gastric Juice enzymology, Gastritis enzymology, Oligopeptides metabolism, Pepsin A metabolism, Vasoactive Intestinal Peptide metabolism
- 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.
- Published
- 1994