Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein
Baldwin, G.S. ; Chandler, R. ; Grego, B. ; Ruibira, M.R. ; Seet, K.L. ; Weinstock, J.
Amsterdam : Elsevier
Amsterdam : Elsevier
ISSN: |
0020-711X
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Keywords: |
Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase
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Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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Topics: |
Biology
Chemistry and Pharmacology
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798290878813437953 |
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autor | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. |
autorsonst | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. |
book_url | http://linkinghub.elsevier.com/retrieve/pii/0020-711X(94)90010-8 |
datenlieferant | nat_lic_papers |
fussnote | 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^1^5]-gastrin; 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 gb-subunit of the gastric H^+/K^+-ATPase.4. The gastrin-binding activity remained in association with p78, and could be separated from the P-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. |
hauptsatz | hsatz_simple |
identnr | NLZ186240422 |
issn | 0020-711X |
journal_name | International Journal of Biochemistry |
materialart | 1 |
package_name | Elsevier |
publikationsort | Amsterdam |
publisher | Elsevier |
reference | 26 (1994), S. 529-538 |
schlagwort | Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase |
search_space | articles |
shingle_author_1 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. |
shingle_author_2 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. |
shingle_author_3 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. |
shingle_author_4 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. |
shingle_catch_all_1 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase 0020-711X 0020711X Elsevier |
shingle_catch_all_2 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase 0020-711X 0020711X Elsevier |
shingle_catch_all_3 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase 0020-711X 0020711X Elsevier |
shingle_catch_all_4 | Baldwin, G.S. Chandler, R. Grego, B. Ruibira, M.R. Seet, K.L. Weinstock, J. Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase Gastrin receptor Gastric H^+/K^+-ATPase gb-subunit Enoyl-CoA hydratase 0020-711X 0020711X Elsevier |
shingle_title_1 | Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein |
shingle_title_2 | Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein |
shingle_title_3 | Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein |
shingle_title_4 | Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein |
sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
timestamp | 2024-05-06T08:23:44.313Z |
titel | Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein |
titel_suche | Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein 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^1^5]-gastrin; 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 gb-subunit of the gastric H^+/K^+-ATPase.4. The gastrin-binding activity remained in association with p78, and could be separated from the P-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. |
topic | W V |
uid | nat_lic_papers_NLZ186240422 |