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3. Subsite study of human pepsin in disease

Author

M, Balbaa, E A, Hamed, A, el-Ashwah, O, Salem, and A, Shamss-Eldin

Subjects
Kinetics, Binding Sites, Gastric Juice, Reference Values, Duodenal Ulcer, Gastritis, Molecular Sequence Data, Humans, Amino Acid Sequence, Oligopeptides, Pepsin A, Substrate Specificity, Vasoactive Intestinal Peptide
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

5. 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

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