TY - JOUR
T1 - Steroid 11β-hydroxylase activity in the microsomal fraction of human adrenals
AU - Klein, A.
AU - Siebenmann, R.
AU - Curtius, H. Ch
AU - Zachmann, M.
N1 - Funding Information:
* Supported by the “Schweizerischer Nationatfonds zur Fordenung der wissenschaftlichen Forschung” (Grant No. 3.679.71). t Supported by the “Hoffmann-La Roche Studienstif-tung”.
PY - 1976/4
Y1 - 1976/4
N2 - The conversion of 11-deoxycortisol and 11-deoxycorticosterone (DOC) to their 11β-hydroxylated metabolites was measured in the 20,000 and 105,000 g fractions of human adrenals. The adrenals were obtained from kidney transplantation donors. The results indicate the presence of relatively high 11β-hydroxylase activity in the microsomal fraction which cannot be attributed to enzyme contamination. In addition there would seem to be further metabolism of cortisol probably by an 17α-hydroxysteroid side chain cleavage enzyme.
AB - The conversion of 11-deoxycortisol and 11-deoxycorticosterone (DOC) to their 11β-hydroxylated metabolites was measured in the 20,000 and 105,000 g fractions of human adrenals. The adrenals were obtained from kidney transplantation donors. The results indicate the presence of relatively high 11β-hydroxylase activity in the microsomal fraction which cannot be attributed to enzyme contamination. In addition there would seem to be further metabolism of cortisol probably by an 17α-hydroxysteroid side chain cleavage enzyme.
UR - http://www.scopus.com/inward/record.url?scp=0017101078&partnerID=8YFLogxK
U2 - 10.1016/0022-4731(76)90128-X
DO - 10.1016/0022-4731(76)90128-X
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AN - SCOPUS:0017101078
SN - 0022-4731
VL - 7
SP - 283
EP - 287
JO - Journal of Steroid Biochemistry
JF - Journal of Steroid Biochemistry
IS - 4
ER -