PURIFICATION AND AMINO-ACID-SEQUENCE OF VASOACTIVE-INTESTINAL-PEPTIDE, PEPTIDE HISTIDINE ISOLEUCINAMIDE (1-27) AND SECRETIN FROM THE SMALL-INTESTINE OF GUINEA-PIG

被引：15

作者：

BUSCAIL, L ^{[1
]}

CAUVIN, A ^{[1
]}

GOURLET, P ^{[1
]}

GOSSEN, D ^{[1
]}

DENEEF, P ^{[1
]}

RATHE, J ^{[1
]}

ROBBERECHT, P ^{[1
]}

VANDERMEERSPIRET, MC ^{[1
]}

VANDERMEERS, A ^{[1
]}

CHRISTOPHE, J ^{[1
]}

机构：

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

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1038卷 / 03期

关键词：

(Guinea pig); Neuropeptide; Peptide histidine isoleucinamide; Secretin; Sequence analysis; Vasoactive intestinal peptide;

D O I：

10.1016/0167-4838(90)90248-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The neuropeptides vasoactive intestinal peptide (VIP) and peptide histidine isoleucinamide (1-27) (PHI) and the hormone secretin were purified from the small intestine of guinea pig, being detected by radioimmunoassay and radioreceptor assay throughout six to seven chromatographic steps. After elution on a reverse-phase C18 column, the three peptides were separated on a Fractogel column. After cation-exchange chromatography of each peptide on Mono S, the final steps were performed using a reverse-phase RP8-e column. Guinea pig PHI differed from porcine PHI in having Tyr and Arg residues instead of Phe and Lys in, respectively, position 10 and 20. We confirmed the original sequence of guinea pig VIP previously documented (with Leu5, Thr9, Met19 and Val26). We also established the similarity of the primary structure of guinea pig secretin with that of porcine and bovine. © 1990.

引用

页码：355 / 359

页数：5

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