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Abstract:

Epididymal 5α reductase activity was found distributed in the crude nuclear fraction (44%) and microsomal fraction (41%). Spermatozoa contaminating the nuclear preparation accounted for only 3% of its activity. There were no regional differences in the distribution of total 5α reductase activity. However, the nuclear enzyme was more active in caput than in other regions. Maximal activity was found at pH 6.2 and at 32°C. Both enzymes had an absolute requirement of reduced dinucleotides. The microsomal preparation could only use NADPH while the nuclear enzyme could use NADPH and NADH. The apparent Km for the microsomal preparation was 0.62 ± 0.05 × 10-6M and Vmax was 555 ± 38 pmoles/mg protein/hour. The nuclear enzyme presented similar values. The reaction was not inhibited by accumulation of product in the medium, but other steroids such as progesterone, epitestosterone(17α-hydroxy-4-androsten-3-one) and 3-oxo-4-androstene-17β-carboxylic acid were potent competitive inhibitors. The reaction was strongly inhibited by Hg, Zn and Cu. The properties of the epididymal reductase are similar to those of the prostatic enzyme. © 1977.

Registro:

Documento: Artículo
Título:Partial characterization of epididymal 5α reductase in the rat
Autor:Monsalve, A.; Blaquier, J.A.
Filiación:Laboratorio de Esteroides, Instituto de Biologia y Medicina Experimental, Obligado 2490, Buenos Aires, 1428, Argentina
Palabras clave:steroid reductase; divalent cation; nicotinamide adenine dinucleotide phosphate; oxidoreductase; steroid 5alpha reductase; Testosterone 5 alpha Reductase; enzyme localization; epididymis; in vitro study; rat; theoretical study; animal; article; cell fractionation; enzymology; epididymis; kinetics; male; metabolism; pH; spermatozoon; temperature; Animal; Cations, Divalent; Epididymis; Hydrogen-Ion Concentration; Kinetics; Male; NADP; Oxidoreductases; Rats; Spermatozoa; Subcellular Fractions; Temperature; Testosterone 5-alpha-Reductase
Año:1977
Volumen:30
Número:1
Página de inicio:41
Página de fin:51
DOI: http://dx.doi.org/10.1016/0039-128X(77)90135-0
Título revista:Steroids
Título revista abreviado:Steroids
ISSN:0039128X
CODEN:STEDA
CAS:steroid reductase, 42616-29-5, 9082-73-9; nicotinamide adenine dinucleotide phosphate, 53-59-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; Cations, Divalent; NADP, 53-59-8; Oxidoreductases, EC 1.; Testosterone 5-alpha-Reductase, EC 1.3.99.5
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0039128X_v30_n1_p41_Monsalve

Referencias:

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Citas:

---------- APA ----------
Monsalve, A. & Blaquier, J.A. (1977) . Partial characterization of epididymal 5α reductase in the rat. Steroids, 30(1), 41-51.
http://dx.doi.org/10.1016/0039-128X(77)90135-0
---------- CHICAGO ----------
Monsalve, A., Blaquier, J.A. "Partial characterization of epididymal 5α reductase in the rat" . Steroids 30, no. 1 (1977) : 41-51.
http://dx.doi.org/10.1016/0039-128X(77)90135-0
---------- MLA ----------
Monsalve, A., Blaquier, J.A. "Partial characterization of epididymal 5α reductase in the rat" . Steroids, vol. 30, no. 1, 1977, pp. 41-51.
http://dx.doi.org/10.1016/0039-128X(77)90135-0
---------- VANCOUVER ----------
Monsalve, A., Blaquier, J.A. Partial characterization of epididymal 5α reductase in the rat. Steroids. 1977;30(1):41-51.
http://dx.doi.org/10.1016/0039-128X(77)90135-0