Regulation of rat liver microsomal cholesterol 7α-hydroxylase by MgATP: Effect of pH

Kwok C.T., Praga Pillay S. and Hardie I.R. (1983) Regulation of rat liver microsomal cholesterol 7α-hydroxylase by MgATP: Effect of pH. Biochemical and Biophysical Research Communications, 116 3: 966-973. doi:10.1016/S0006-291X(83)80236-8


Author Kwok C.T.
Praga Pillay S.
Hardie I.R.
Title Regulation of rat liver microsomal cholesterol 7α-hydroxylase by MgATP: Effect of pH
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 1090-2104
Publication date 1983-11-15
Sub-type Article (original research)
DOI 10.1016/S0006-291X(83)80236-8
Volume 116
Issue 3
Start page 966
End page 973
Total pages 8
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract Cholesterol 7α-hydroxylase when assayed under conditions that favour phosphorylation can be activated or inactivated by MgATP, depending on ATP concentration and the pH of the incubation medium. Maximum stimulation of 7α-hydroxylase was obtained with 0.5 mM ATP in both acidic and alkaline pH. At a pH lower than 7.4, 7α-hydroxylase was inactivated by 2.0 and 3.0 mM MgATP. The inactivation by 3 mM MgATP was significantly greater at pH 6.7 than pH 7.4. Protein kinases enhanced these effects, suggesting covalent modification of the enzyme by phosphorylation. These findings are consistent with a protein kinase catalyzed phosphorylation, and suggest that MgATP may have a dual role in the activation and inactivation of 7α-hydroxylase in vivo.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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Created: Tue, 12 Jul 2016, 12:36:11 EST by System User