The influence of the side chain on sterol side-chain cleavage in rat adrenal glands.
Biochim Biophys Acta
; 711(1): 123-7, 1982 Apr 15.
Article
en En
| MEDLINE
| ID: mdl-6896004
The cholesterol side-chain cleavage enzyme system of rat adrenal cortex, the enzyme catalyzing a rate-limiting step of adrenal steroidogenesis, was shown to metabolize a series of cholesterol analogues to pregnenolone. In the presence of Ca2+, rat adrenocortical mitochondria converted the analogue with two less methylene groups (C25) than cholesterol into pregnenolone at a faster rate than cholesterol. The analogues with one or three less methylene groups (C26 or C24) were metabolized at a similar rate to cholesterol. Lengthening the non-polar side chain produced analogues that did not appear to be metabolized. Studies of the metabolism of these analogues in isolated rat adrenocortical carcinoma cells showed that the C24 and C25 analogues were converted into pregnenolone much more efficiently than was cholesterol or the C26 sterol. The experimental findings are explained in terms of the differing ability of each exogenously added sterol to gain access to the active site of the sterol side-chain cleavage enzyme by passage through the membranes of the adrenal cell.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oxidorreductasas
/
Enzima de Desdoblamiento de la Cadena Lateral del Colesterol
/
Glándulas Suprarrenales
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1982
Tipo del documento:
Article
Pais de publicación:
Países Bajos