Abstract
Abstract.
The binding of 5α-dihydroprogesterone (DHP)1 to proteins in pregnancy serum has been investigated and compared with the binding of progesterone. Characteristic properties of the DHP-serum protein interaction were unsaturability, low affinity and poor complex stability. Fractionation of serum using a variety of protein separation techniques, revealed that DHP interacts with several proteins. At low temperature (0–4°C) albumin appeared to be the principal binding component whereas higher temperatures seemed to favour binding to β-lipoproteins and α2-macroglobulin. Binding to specific binding proteins such as the corticosteroid binding globulin (CBG) and the sex hormone-binding globulin, (SHBG) were detectable but appeared to be quantitatively unimportant.
Progesterone showed a similar multicomponent interaction but differed from DHP in the extent of binding to CBG. Binding of either hormone to the α1-acid-glycoprotein was negligible.
The present study shows that the high endogenous DHP levels present in pregnancy sera are caused by factors other than high affinity protein binding.
Subject
Endocrinology,General Medicine,Endocrinology, Diabetes and Metabolism
Cited by
2 articles.
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