Cholesterol 7α‐hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation
L B Nguyen, S Shefer, G Salen, J Y Chiang, M Patel – 1 December 1996 – Purified cholesterol 7α‐hydroxylases (C7αH) from human and rat liver microsomes, and from transformed Escherichia coli expression systems, were incubated with 0.3 mmol/L [gamma‐32P] adenosine triphosphate (ATP) in the presence and absence of bacterial alkaline phosphatase (AP) or rabbit muscle adenosine 3′,5′‐cyclic monophosphate (cAMP)‐dependent protein kinase.