TY - JOUR
T1 - The topology of the mitochondrial 11β-hydroxylase system in bovine adrenal cortex
AU - Rydström, J.
AU - Gustafsson, J. Å
AU - Ingelman-Sundberg, M.
AU - Montelius, J.
AU - Ernster, L.
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1976/12/6
Y1 - 1976/12/6
N2 - Binding of deoxycorticosterone to cytochrome P-450 of the 11β-hydroxylase system in adrenal cortex mitochondria was inhibited by the nonpenetrating protein reagent diazobenzenesulfonate in damaged but not in intact mitochondria. The slowly penetrating hydrophilic substrate deoxycorticosterone 21-sulfate showed a slow binding to cytochrome P-450 as compared to the hydrophobic nonesterified steroid. In contrast, the esterified and nonesterified steroids bound equally fast in sonicated, aged or lysolecithin-treated mitochondria. These data imply that the steroid substrates must penetrate the inner mitochondrial membrane to interact with the 11β-hydroxylase system.
AB - Binding of deoxycorticosterone to cytochrome P-450 of the 11β-hydroxylase system in adrenal cortex mitochondria was inhibited by the nonpenetrating protein reagent diazobenzenesulfonate in damaged but not in intact mitochondria. The slowly penetrating hydrophilic substrate deoxycorticosterone 21-sulfate showed a slow binding to cytochrome P-450 as compared to the hydrophobic nonesterified steroid. In contrast, the esterified and nonesterified steroids bound equally fast in sonicated, aged or lysolecithin-treated mitochondria. These data imply that the steroid substrates must penetrate the inner mitochondrial membrane to interact with the 11β-hydroxylase system.
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U2 - 10.1016/0006-291X(76)90846-9
DO - 10.1016/0006-291X(76)90846-9
M3 - Article
C2 - 1008873
AN - SCOPUS:0017102019
VL - 73
SP - 555
EP - 561
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -