Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma.
The primary structure of a human pancreastatin-like peptide was determined from a pancreatic glucagonoma. The 28-amino acid peptide was identified using a specific antibody raised against porcine pancreastatin 1-49 and showed a 75% sequence homology with porcine pancreastatin 22-49 and bovine chromogranin A 267-294. Several forms of pancreastatin-like immunoreactivity were found in human endocrine tumors of which the purified peptide was the smallest and contained the active sequence of pancreastatin.
Sekiya
K
K
Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, England.
Ghatei
M A
MA
Minamino
N
N
Bretherton-Watt
D
D
Matsuo
H
H
Bloom
S R
SR
D007516:Adenoma, Islet Cell / Q000032:analysis*; D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000032:analysis; D000918:Antibody Specificity; D002417:Cattle; D053379:Chromogranin A; D005260:Female; D005935:Glucagonoma / Q000032:analysis*; D006801:Humans; D008875:Middle Aged; D010187:Pancreatic Hormones / Q000032:analysis* / Q000276:immunology; D010190:Pancreatic Neoplasms / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis* / Q000276:immunology; D013552:Swine
D000906:Antibodies; D053379:Chromogranin A; D010187:Pancreatic Hormones; D010446:Peptide Fragments; C050836:pancreastatin