Affinity chromatography of estrogen- and progesterone-binding proteins of human uterus |
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Authors: | M Thapar P Sujata G L Kumari T G Shrivastava S K Sachdeva |
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Institution: | (1) Department of Reproductive Biomedicine, National Institute of Health and Family Welfare, 110 067 Munirka, New Delhi, India;(2) Department of Obstetrics and Gynaecology, Safdarjung Hospital, 110 016 New Delhi, India |
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Abstract: | The purification of estrogen- and progesterone-binding proteins of human uterus by employing affinity resins coupled with
steroid-bovine serum albumin conjugates, led to the isolation of preparations with estrogen- and progesterone-binding sites
havingK
d values in the range of 0.96 to 1.20 × 10-9 M. These were different from theK
d values of 10-10 M and 10-8 M obtained for two types of binding sites present in the crude cytosolic and nuclear fractions. The purified proteins sedimented
on sucrose gradient withS values in the range of 3.6–4.4.
The cytosolic and nuclear estrogen- and progesterone-binding proteins, thus purified, showed differences in specificity of
binding to the hormone. While the cytoplasmic proteins were more specific in their binding to estradiol or progesterone, the
nuclear proteins bound Cortisol with equal or moderate affnity. These results demonstrate the presence of distinct physiological
forms of estrogen- and progesterone-binding proteins in the cytoplasm and nucleus, thus pointing to the importance of both
these compartments in hormone action. |
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Keywords: | Human uterus estrogen-binding protein progesterone-binding protein affnity chromatography |
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