Isolation and characterization of bovine pancreastatin.
Bovine pancreastatin, a 47 amino acid residue peptide, was isolated from the pancreas and the pituitary gland using a chemical method which detects its C-terminal glycine amide structure. The complete amino acid sequence of the pancreatic peptide is 74% homologous to that of porcine pancreastatin and is identical to bovine chromogranin A-(248-294), as deduced from its cDNA sequence. The sequence of the first 28 amino-terminal residues of the pituitary peptide was determined to be identical to the corresponding sequence of the pancreatic peptide. Since the pituitary peptide also contains the C-terminal glycine amide, it is therefore likely to be identical in structure to the pancreatic peptide. Thus, we conclude that bovine chromogranin A is the precursor of bovine pancreastatin. Synthetic bovine pancreastatin inhibited pancreatic exocrine secretion in a similar manner to porcine pancreastatin.
Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, CA 94305.
I
I
Nakano
A
A
Funakoshi
K
K
Miyasaka
K
K
Ishida
G
G
Makk
P
P
Angwin
D
D
Chang
K
K
Tatemoto
D000818:Animals; D002417:Cattle; D002766:Cholecystokinin / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D053379:Chromogranin A; D006801:Humans; D008297:Male; D010179:Pancreas / Q000032:analysis* / Q000187:drug effects / Q000378:metabolism; D010187:Pancreatic Hormones / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D010902:Pituitary Gland / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains; D013552:Swine
D053379:Chromogranin A; D010187:Pancreatic Hormones; C050836:pancreastatin; D002766:Cholecystokinin