Related Experiment Videos
Subsite study of human pepsin in disease
M Balbaa1, E A Hamed, A el-Ashwah
1Department of Biochemistry, Faculty of Science, Alexandria University, Egypt.
Indian Journal of Biochemistry & Biophysics
|April 1, 1994
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.