Hampton, B. S., Marshak, D. R., Burgess, W. H. (January 1992) Structural and functional characterization of full-length heparin-binding growth associated molecule. Mol Biol Cell, 3 (1). pp. 85-93. ISSN 1059-1524 (Print)1059-1524 (Linking)
Abstract
Heparin-binding growth-associated molecule (HB-GAM) was purified from adult bovine brain and chicken heart. The yield of HB-GAM is increased by 5- to 10-fold when 250 mM NaCl is added to the homogenization buffer, indicating that HB-GAM may exist as a complex with an insoluble component of the tissue. The complete amino acid sequence of the brain-derived HB-GAM was established by automated Edman degradation of the intact protein and chemically or enzymatically derived fragments. The mass of bovine HB-GAM as determined by plasma desorption time-of-flight mass spectrometry is 15,291 mass units, which compares favorably with the calculated mass of 15,289 based on the amino acid sequence. Therefore, HB-GAM has not undergone any major post-translational modifications other than cleavage of the signal peptide. These results indicate that previous amino acid sequence analysis of this protein was carried out using truncated HB-GAM. Full-length HB-GAM is not a mitogen for Balb/3T3 clone A31, Balb MK, NRK, or human umbilical vein endothelial cells. HB-GAM does, however, have adhesive properties and neurite extension activity for chick embryo cerebral cortical derived neurons when presented to these cells as a substrate. HB-GAM had little neurite extension activity when presented as a soluble factor.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | 3T3 Cells Amino Acid Sequence Animals Brain Chemistry Carrier Proteins/*chemistry/isolation & purification Cattle Cell Division/drug effects Cells, Cultured Chickens Cytokines/*chemistry/isolation & purification Electrophoresis, Polyacrylamide Gel Growth Substances/*chemistry/isolation & purification/pharmacology Humans Mice Mitogens/pharmacology Molecular Sequence Data Molecular Weight Myocardium/chemistry Neurites/drug effects/physiology Sodium Chloride |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification Investigative techniques and equipment > spectroscopy > mass spectrometry bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization |
| CSHL Authors: | |
| Communities: | CSHL labs |
| Depositing User: | Matt Covey |
| Date: | January 1992 |
| Date Deposited: | 29 Sep 2015 14:50 |
| Last Modified: | 29 Sep 2015 14:50 |
| PMCID: | PMC275504 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/31818 |
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