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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Veeraragavan K,Coulombe R,Gagnon Cdoi
10.1016/s0006-291x(88)80099-8subject
Has Abstractpub_date
1988-04-29 00:00:00pages
732-8issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(88)80099-8journal_volume
152pub_type
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