合成人胰抑制素对外分泌胰腺的生物活性。

Bioactivity of synthetic human pancreastatin on exocrine pancreas.

作者信息

Funakoshi A, Miyasaka K, Nakamura R, Kitani K, Funakoshi S, Tamamura H, Fujii N, Yajima H

机构信息

National Kyushu Cancer Center, Fukuoka, Japan.

出版信息

Biochem Biophys Res Commun. 1988 Nov 15;156(3):1237-42. doi: 10.1016/s0006-291x(88)80765-4.

DOI:10.1016/s0006-291x(88)80765-4

PMID:3190702

Abstract

A biological activities of synthetic human pancreastatin (1-52) and its C-terminal fragment (24-52) were evaluated for the first time in the conscious rats. Both pancreastatins inhibited CCK-stimulated pancreatic secretion in a range of 20-200 pmol/kg/h with the same potency, indicating that the C-terminal portion of this peptide has a full biological activity. The relative molar potency of this substance compared to that of porcine pancreastatin was equivalent. This study suggests that human pancreastatin has the same biological activity as that of porcine, and plays a biological action in the exocrine pancreas.

摘要

首次在清醒大鼠中评估了合成人胰抑制素（1-52）及其C末端片段（24-52）的生物学活性。两种胰抑制素均以相同效力在20-200 pmol/kg/h范围内抑制胆囊收缩素刺激的胰腺分泌，表明该肽的C末端部分具有完整的生物学活性。该物质与猪胰抑制素相比的相对摩尔效力相当。本研究表明，人胰抑制素与猪胰抑制素具有相同的生物学活性，并在外分泌胰腺中发挥生物学作用。