PURIFICATION AND AMINO-ACID-SEQUENCE OF VASOACTIVE-INTESTINAL-PEPTIDE, PEPTIDE HISTIDINE ISOLEUCINAMIDE AND SECRETIN FROM THE OVINE SMALL-INTESTINE

被引：11

作者：

BOUNJOUA, Y ^{[1
]}

VANDERMEERS, A ^{[1
]}

ROBBERECHT, P ^{[1
]}

VANDERMEERSPIRET, MC ^{[1
]}

CHRISTOPHE, J ^{[1
]}

机构：

[1] FREE UNIV BRUSSELS,SCH MED,DEPT BIOCHEM & NUTR,BLVD WATERLOO 115,B-1000 BRUSSELS,BELGIUM

来源：

REGULATORY PEPTIDES | 1991年 / 32卷 / 02期

关键词：

VASOACTIVE INTESTINAL PEPTIDE; PEPTIDE HISTIDINE ISOLEUCINAMIDE; SECRETIN; OVINE SMALL INTESTINE;

D O I：

10.1016/0167-0115(91)90044-H

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Vasoactive intestinal peptide (VIP), peptide histidine isoleucinamide (PHI) and secretin were separated and purified to homogeniety from ovine small intestine, using radioimmunoassay and radioreceptor assay for detection. An efficient and rapid purification sequence included acid extraction, concentration on a bulk C18 cartridge, filtration on a Fractogel column, ion-exchange chromatography on Mono-S and a maximum of three successive reverse-phase HPLC steps. The amounts of peptides obtained from 450 g wet weight tissue were 20-mu-g VIP, 15-mu-g PHI and 5-mu-g secretin. The as yet unknown amino acid sequences of the three peptides were found to be identical to those of the corresponding bovine peptides.

引用

页码：169 / 179

页数：11

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