| Autor: |
Quemener, E., Amet, Y., Fournier, G., Distefano, S., Abalain, J.H., Floch, H.H. |
| Zdroj: |
Biochemical and Biophysical Research Communications; November 1994, Vol. 205 Issue: 1 p269-274, 6p |
| Abstrakt: |
5α-reductase 2 from human prostate solubilized into an active and stable form using a non-ionic detergent octylglucoside was successfully purified using a four-step chromatographic procedure. The enzyme was obtained as an apparently homogeneous protein exhibiting an apparent molecular weight of 42 kDa upon SDS-PAGE. Con A, DBA, UEA-I, and RCA60lectins recognized this protein. After treatment with O-glycosidase and neuraminidase, a protein of an apparent molecular weight about 30 kDa appeared. On the other hand, N-glycosidase treatment of this enzyme had no effect. These results indicate that the human prostate testosterone 5α-reductase 2 is an O-glycosylated sialoglycoprotein with a peptide moiety of about 30 kDa; the oligosaccharide side chains contain mannose, N-acetyl galactosamine, fucose, galactose and sialic acids. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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