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J. Biol. Chem., Vol. 259, Issue 8, 4885-4889, 04, 1984
LT Duong, PJ Fleming and JT Russell
An identical cytochrome b561 was found to be an integral component of both
chromaffin vesicles from adrenal medulla and neurosecretory vesicles from
posterior pituitary by spectrophotometric and immunological techniques. The
neurosecretory vesicles had 6.8 micrograms of cytochrome/mg of membrane
protein versus 69 micrograms/mg in chromaffin vesicles. This cytochrome was
also immunologically detected in various regions of bovine brain and was
immunologically distinct from the cytochrome found in serotonin-containing
vesicles from platelets. Dopamine beta-hydroxylase involved in the
biosynthesis of catecholamines was not present in neurosecretory vesicles,
suggesting an alternative functional role for the cytochrome in these
vesicles. Neurosecretory vesicles do contain a mixed function oxidase
(peptidyl alpha-amidase) which appears to be involved in alpha- amidation
of the carboxyl termini of vasopressin and oxytocin. We suggest that
cytochrome b561 in the two vesicles may be functionally associated with
different ascorbic acid-dependent, copper-containing mixed function
oxidases: dopamine beta-hydroxylase and peptidyl alpha- amidase.
An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles
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