ISOLATION AND PARTIAL AMINO-ACID-SEQUENCE OF A 78 KDA PORCINE GASTRIN-BINDING PROTEIN
Details
Publication Year 1994-04, Volume 26, Issue #4, Page 529-538
Journal Title
INTERNATIONAL JOURNAL OF BIOCHEMISTRY
Publication Type
Journal Article
Abstract
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.
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Keywords
CHOLECYSTOKININ RECEPTOR; PARIETAL-CELLS; BETA-SUBUNIT; FUNCTIONAL EXPRESSION; AUTOIMMUNE GASTRITIS; CROSS-LINKING; H+/K+-ATPASE; CLONING; IDENTIFICATION; PURIFICATION
Rights Notice
Refer to copyright notice on published article.


Creation Date: 1994-04-01 12:00:00
Last Modified: 0001-01-01 12:00:00
An error has occurred. This application may no longer respond until reloaded. Reload 🗙