Stoichiometric carboxyl methylation of chromogranins from bovine adrenal medullary cells.

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.

authors

Veeraragavan K,Coulombe R,Gagnon C

doi

10.1016/s0006-291x(88)80099-8

subject

Has Abstract

pub_date

1988-04-29 00:00:00

pages

732-8

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80099-8

journal_volume

152

pub_type

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