| Autor: |
Virsolvy-Vergine, A., Salazar, G., Sillard, R., Denoroy, L., Mutt, V., Bataille, D. |
| Zdroj: |
Diabetologia; Feb1996, Vol. 39 Issue 2, p135-141, 7p |
| Abstrakt: |
Anti-diabetic sulphonylureas act via high affinity binding sites coupled to K-ATP channels. Endosulfine, an endogenous ligand for these binding sites, was shown to exist in two molecular forms, α and Β, in both the pancreas and the central nervous system. We describe here the isolation, and partial structural characterization of α endosulfine derived from porcine brains by means of a series of chromatography runs and gel electrophoresis. Porcine α endosulfine is a protein with a molecular mass of 13,196 daltons as determined by mass spectrometry and which is N-terminally blocked. Tryptic digestion followed by separation of the fragments by HPLC and automated Edman degradation yielded a total of 72 amino acids in four partial sequences. Comparison of these sequences with that present in the National Biomedical Research Foundation protein data bank indicated a 82% identity with a 112-amino acid protein with a molecular mass of 12,353 daltons called 'cyclic AMP-regulated phosphoprotein-19', isolated from the bovine brain as a substrate for protein kinase A. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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