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- W1567416586 abstract "We have shown that purified bovine soluble dopamine β-hydroxylase can reconstitute onto preformed phosphatidylserine containing vesicles. The binding is dependent on pH and vesicle phosphatidylserine composition but does not require calcium. Reconstitution appears to be irreversible, with the lipid-bound enzyme possessing hydroxylase activity. Additionally, [14C] phosphatidylserine binds to soluble dopamine β-hydroxylase and remains bound after several detergent washes. Thus the reconstituted soluble form of the enzyme appears to be functionally analogous to the membranous form. Both the reconstitution data and the lipid binding data suggest that multiple phosphatidylserine molecules bind to the soluble hydroxylase. We propose that noncovalently bound phosphatidylserine moieties, which copurify with the membrane bound form of the enzyme, alone are responsible for anchoring membranous dopamine β-hydroxylase to chromaffin granule and model membranes." @default.
- W1567416586 created "2016-06-24" @default.
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- W1567416586 date "1989-09-01" @default.
- W1567416586 modified "2023-09-26" @default.
- W1567416586 title "Conversion of soluble dopamine β-hydroxylase to a membrane binding form" @default.
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- W1567416586 doi "https://doi.org/10.1016/s0021-9258(19)84816-0" @default.
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