Subsite study of human pepsin in disease.
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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Oligopeptides
/
Reference Values
/
Substrate Specificity
/
Binding Sites
/
Humans
/
Vasoactive Intestinal Peptide
/
Molecular Sequence Data
/
Kinetics
/
Pepsin A
/
Amino Acid Sequence
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1994
Type:
Article
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