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- W1995851605 abstract "Abstract It has been described previously that human erythrocytes contain steroid dehydrogenase activities and that erythrocytes can bind steroids. In the present studies the binding of steroids by human erythrocyte fractions (haemoglobin-containing membranes, haemoglobin-free membranes, the membrane-free haemolysate, a membrane protein preparation and a 17β-hydroxysteroid dehydrogenase preparation) was investigated by equilibrium dialysis. 1. 1. The membrane protein preparation showed the highest combining affinity for testosterone. The binding sites of all the membrane preparations could not be saturated with testosterone. In the sequence of Δ 5 - pregnenolone , 20α-dihydroprogesterone, progesterone, oestradiol, Δ 5 - androstenediol and testosterone a decrease in combining affinity of haemoglobin-free membranes for the steroids was observed. 2. 2. The binding of testosterone by the membrane-free haemolysate showed a lower combining affinity than the value obtained with the membrane preparations for this steroid. 3. 3. Testosterone was bound in a specific way by a fraction from the membrane free haemolysate, containing 17β-hydroxysteroid dehydrogenase activity. An apparent association constant for binding of testosterone by this fraction was found to be in the order of magnitude of 108 M−1. This enzyme fraction was further characterized by gel chromatography." @default.
- W1995851605 created "2016-06-24" @default.
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- W1995851605 date "1972-08-01" @default.
- W1995851605 modified "2023-09-25" @default.
- W1995851605 title "Localization and characterization of steroid binding sites of human red blood cells" @default.
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- W1995851605 doi "https://doi.org/10.1016/0005-2736(72)90185-x" @default.
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