scholarly journals Editorial: Steroid Transformation Enzymes as Critical Regulators of Steroid Actionin Vivo

Endocrinology ◽  
2000 ◽  
Vol 141 (5) ◽  
pp. 1587-1589 ◽  
Author(s):  
Wen-Chao Song ◽  
Michael H. Melner
1981 ◽  
Vol 11 (2) ◽  
pp. 81-88 ◽  
Author(s):  
Toshiomi Yoshida ◽  
Masaki Sueki ◽  
Hisaharu Taguchi ◽  
Songsri Kulprecha ◽  
Naline Nilubol

1984 ◽  
Vol 30 (1) ◽  
pp. 57-62 ◽  
Author(s):  
J. Długoński ◽  
L. Sedlaczek ◽  
A. Jaworski

Protoplasts were obtained from Hyphoderma roseum (Fries) and Cunninghamella elegans (Lendner), fungi capable of steroid 11-hydroxylation. The lytic enzyme preparation was derived from Trichoderma viride CBS 354-33. Homogeneous protoplast suspension, free of mycelial debris and cell wall fragments, transformed cortexolone and 6α-fluorocortexolone-16,17-acetonide to the same products as the intact mycelium of the microorganisms. Liberation of protoplasts and their stabilizaiton during steroid transformation was the most effective in 0.8 M MgSO4; still, this compound impaired steroid hydroxylation. Consequently, the concentration of the transformation product formed was nearly the same as in sucrose, mannitol, and sorbitol, compounds which caused no inhibition but which were less effective stabilizers.


1955 ◽  
Vol 3 (6) ◽  
pp. 372-374
Author(s):  
Eugene L. Dulaney ◽  
W. J. McAleer ◽  
H. R. Barkemeyer ◽  
Charles Hlavac

1980 ◽  
Vol 3 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Doo Ha Kim ◽  
S. B. Lee ◽  
Dewey D. Y. Ryu

1992 ◽  
Vol 8 (4) ◽  
pp. 399-401 ◽  
Author(s):  
P. K. Roy ◽  
A. W. Khan ◽  
J. Kumar ◽  
S. D. K. Chopra ◽  
S. K. Basu

1965 ◽  
Vol 11 (2) ◽  
pp. 351-364 ◽  
Author(s):  
Kartar Singh ◽  
S. N. Sehgal ◽  
Claude Vezina

Spores of Septomyxa affinis transformed Reichstein"s compound "S" into mainly 1-dehydro "S" and small amounts of 17-side-chain degradation products. 1-Dehydrogenating activity of the spores was not influenced by the sporulation medium. Adaptation has never been observed. Metal ions, chelating agents, activators, and cofactors showed no significant influence, within wide limits. Externally supplied phosphate, glucose, or any other carbon source was not required. Mercuric chloride, N-ethylmaleimide, NaN3, 2,4-dinitrophenol, antimycin, and some oxidation–reduction dyes inhibited steroid conversion. Degradation of the side chain was blocked by conducting the transformation at 32 °C.Spores of S. affinis oxidized acetate, glucose, fructose, ethanol, and xylose. Oxidation of these substrates was inhibited by most of the reagents that also inhibited steroid transformation.


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