An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles.
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.[1]References
- An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles. Duong, L.T., Fleming, P.J., Russell, J.T. J. Biol. Chem. (1984) [Pubmed]
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