Subsite study of human pepsin in disease.
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.
Balbaa
M
M
Department of Biochemistry, Faculty of Science, Alexandria University, Egypt.
Hamed
E A
EA
el-Ashwah
A
A
Salem
O
O
Shamss-Eldin
A
A
D000595:Amino Acid Sequence; D001665:Binding Sites; D004381:Duodenal Ulcer / Q000201:enzymology*; D005750:Gastric Juice / Q000201:enzymology*; D005756:Gastritis / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D010434:Pepsin A / Q000378:metabolism*; D012016:Reference Values; D013379:Substrate Specificity; D014660:Vasoactive Intestinal Peptide / Q000378:metabolism*
D009842:Oligopeptides; D014660:Vasoactive Intestinal Peptide; D010434:Pepsin A