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Stoichiometric carboxyl methylation of chromogranins from bovine adrenal medullary cells.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1988 Apr 29; Vol. 152 (2), pp. 732-8. - Publication Year :
- 1988
-
Abstract
- The secretory proteins from adrenal chromaffin granules, chromogranins A, A1 and A2, were found to be excellent in vitro methyl acceptor proteins. The purified protein-carboxyl methylase (PCM) from bovine erythrocytes incorporated 660, 2540 and 7890 pmol of methyl group/10 min/mg protein in chromogranins A, A1 and A2, respectively. However, dopamine beta-hydroxylase, another secretory protein within chromaffin granules was poorly methylated. The stoichiometry of methylation for chromogranins A, A1 and A2 was 0.26, 0.89 and 1.3 mol of methyl group/mol of protein, respectively. Kinetic analysis showed that chromogranins A1 had the highest turnover rate followed by chromogranins A2 and A. These chromogranins are the first secretory proteins to be stoichiometrically methylated in vitro without prior deamidation.
- Subjects :
- Adrenal Medulla cytology
Animals
Cattle
Dopamine beta-Hydroxylase isolation & purification
Dopamine beta-Hydroxylase metabolism
Electrophoresis, Polyacrylamide Gel
Kinetics
Methylation
Protein Methyltransferases metabolism
Substrate Specificity
Adrenal Medulla metabolism
Chromogranins metabolism
Nerve Tissue Proteins metabolism
Protein Methyltransferases isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 152
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 3365250
- Full Text :
- https://doi.org/10.1016/s0006-291x(88)80099-8