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胰抑素(Pancreastatin)最初是从猪胰腺中获得的,为49肽激素,该肽C末端具有特殊的甘氨酰胺结构,通常检出此结构的存在即可进一步分离纯化。此肽对葡萄糖和精氨酸引起的胰岛素分泌是强烈的抑制剂,提示其在胰岛素分泌中起重要的调节作用。胰抑素也抑制CCK刺激引起的胰腺外分泌。猪胰抑素的基本结构与一种存在于许多内分泌细胞的分泌性糖蛋白——Chromogranin A的结构很相似。为弄清两者的关系,美国斯坦福大学医学院精神病和行为科学系,加州半岛实验室、日本福冈国立癌症中心和东京都老年病研究所第一临床生理实验室的科学家们合作,从牛胰腺中分离提取了牛胰抑素,为47肽,此肽整个氨基酸序列的47％与猪胰抑素相同,而且从它的cDNA序列推断,与牛的chromogranin A-(248～294)
Pancreastatin, originally obtained from porcine pancreas, is a 49-peptide hormone with a specific glycinamide structure at its C-terminus. This construct is usually detected for further isolation and purification. This peptide is a potent inhibitor of insulin secretion by glucose and arginine, suggesting that it plays an important regulatory role in insulin secretion. Pancreatin also inhibits pancreatic exocrine secretion induced by CCK stimulation. The basic structure of porcine panostatin is very similar to that of Chromogranin A, a secreted glycoprotein found in many endocrine cells. To understand the relationship between the two, Stanford University School of Medicine Department of Psychiatry and Behavioral Sciences, California Peninsula Laboratory, Japan Fukuoka National Cancer Center and Tokyo Institute of Geriatrics, the first clinical physiology laboratory scientists, from the bovine pancreas Was isolated from bovine pancreatin, which is 47 peptides. The entire amino acid sequence of the peptide is 47% identical to that of porcine panostatin, and deduced from its cDNA sequence that it interacts with chromogranin A- (248-294)