| Purification and characterization of the neu/erb B2 ligand-growth factor from bovine kidney. | |
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MedLine Citation:
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PMID: 1350785 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A neu/erb B2 ligand growth factor (NEL-GF) was purified to homogeneity from bovine kidney by a procedure involving ammonium sulfate fractionation (35-70% saturation) followed by sequential column chromatography on DEAE-cellulose (DE52), Sulfadex (sulfated Sephadex G-50), heparin-Sepharose 4B, and Superdex 75 (fast protein liquid chromatography). NEL-GF was found to be a 25-kDa polypeptide according to the analysis by gel filtration on Superdex 75 and 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. NEL-GF stimulated the tyrosine-specific autophosphorylation of the neu/erb B2 gene product purified by immunoabsorbent and tyrosine-specific phosphorylation of the neu/erb B2 gene product in intact dihydrofolate reductase (DHFR/G-8 cells (NIH 3T3 cells transfected with rat c-neu). NEL-GF also down-regulated the cell surface neu/erb B2 gene product in DHFR/G-8 cells. NEL-GF was mitogenic toward NIH 3T3 cells, DHFR/G-8 cells, A431 cells (human epidermoid carcinoma cells), and SK-BR-3 cells (human breast carcinoma cells) but inactive toward bovine aorta endothelial cells. NEL-GF was sensitive to 0.1% trifluoroacetic acid but resistant to 5% beta-mercaptoethanol and appeared to be distinct from a neu protein-specific activating factor (Davis, J. G., Hamuro, J., Shim, C. Y., Samanta, A., Greene, M. I., and Dobashi, K. (1991) Biochem. Biophys. Res. Commun. 179, 1536-1542) and a 30-kDa glycoprotein which competed with a monoclonal antibody for binding to the neu/erb B2 gene product (Lupu, R., Colomer, R., Zugmaier, G., Sarup, J., Shepard, M., Slamon, D., and Lippman, M. E. (1990) Science 249, 1552-1555). |
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Authors:
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S S Huang; J S Huang |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 267 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1992 Jun |
Date Detail:
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Created Date: 1992-07-06 Completed Date: 1992-07-06 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 11508-12 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, Missouri 63104. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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3T3 Cells Animals Autoradiography Cattle Cells, Cultured Chromatography, Gel Down-Regulation Electrophoresis, Polyacrylamide Gel Endothelium, Vascular / cytology, metabolism Humans Kidney / metabolism* Mice Phosphorylation Protein-Tyrosine Kinases / metabolism* Proto-Oncogene Proteins / isolation & purification*, metabolism Receptor, erbB-2 Tetrahydrofolate Dehydrogenase / metabolism Tumor Cells, Cultured |
| Grant Support | |
ID/Acronym/Agency:
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CA 38808/CA/NCI NIH HHS; HL 41782/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Proto-Oncogene Proteins; EC 1.5.1.3/Tetrahydrofolate Dehydrogenase; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.10.1/Receptor, erbB-2 |
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