Purification and characterization of a steroid-binding sialoglycoprotein from rat ventral prostate
An androgen-dependent sialoglycoprotein was purified from the secretion of rat ventral prostate by chromatofocusing and DEAE-Sepharose column chromatography. It showed a native molecular weight of 47,000 and consisted of two dissimilar subunits with molecular weights of 20,000 and 18,000. However, e...
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| Main Authors: | , |
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| Format: | Article |
| Published: |
2018
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| Online Access: | https://repository.li.mahidol.ac.th/handle/123456789/9667 |
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| Institution: | Mahidol University |
| Summary: | An androgen-dependent sialoglycoprotein was purified from the secretion of rat ventral prostate by chromatofocusing and DEAE-Sepharose column chromatography. It showed a native molecular weight of 47,000 and consisted of two dissimilar subunits with molecular weights of 20,000 and 18,000. However, each subunit contained a common peptide with molecular weight of 16,000. It also contained 442 ± 62 μg sialic acids per milligram protein and bound pregnenolone with a binding affinity of 1.2 μm -1 . Its amino acid composition was similar to those of other known prostatic steroid-binding proteins. Hence, we propose that it is the sialylated form of rat prostatic steroid-binding protein. © 1986. |
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