ISOLATION AND PARTIAL AMINO-ACID-SEQUENCE OF A 78 KDA PORCINE GASTRIN-BINDING PROTEIN

被引：12

作者：

BALDWIN, GS ^{[1
]}

CHANDLER, R ^{[1
]}

GREGO, B ^{[1
]}

RUBIRA, MR ^{[1
]}

SEET, KL ^{[1
]}

WEINSTOCK, J ^{[1
]}

机构：

[1] ROYAL MELBOURNE HOSP,WALTER & ELIZA HALL INST MED RES,LUDWIG INST CANC RES,JOINT PROT STRUCT LAB,MELBOURNE,VIC 3050,AUSTRALIA

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1994年 / 26卷 / 04期

关键词：

GASTRIN RECEPTOR; GASTRIC H+/K+-ATPASE BETA-SUBUNIT; ENOYL-COA HYDRATASE; 3-HYDROXYACYL-COA DEHYDROGENASE;

D O I：

10.1016/0020-711X(94)90010-8

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：

1. A 78 kDa protein (p78) has been partially purified from washed membranes isolated from the corpus of porcine gastric mucosa. The purification was monitored by covalent cross-linking of iodinated [Nle(15)]-gastrin(2,17). 2. A single N-terminal sequence extending for 33 amino acids was obtained from the p78 preparation. Partial sequences totalling 192 amino acids were also obtained from 14 tryptic and 3 Staphylococcal V8 peptides. 3. 10 peptides plus the N-terminal sequence were derived from a previously unsequenced protein which was distantly related to the product of the E. coli fadB gene (Baldwin G. S. (1993) Comp. Biochem. Physiol. 104B, 55-61). The remaining 7 peptides were derived from the beta-subunit of the gastric H+/K+-ATPase. 4. The gastrin-binding activity remained in association with p78, and could be separated from the beta-subunit of the gastric H+/K+-ATPase, during chromatography on tomato lectin-Sepharose. 5. We conclude that p78 binds gastrin, and is a novel member of the enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase family of enzymes.

引用

页码：529 / 538

页数：10

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