Glycosylated nature of testosterone 5 alpha-reductase 2 purified from human prostate.
5 alpha-reductase 2 from human prostate solubilized into an active and stable form using a non-ionic detergent octyl glucoside 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 RCA60 lectins 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 5 alpha-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.
Quemener
E
E
Département de Biochimie et Biologie Moléculaire, Faculté de Médecine, Brest, France.
Amet
Y
Y
Fournier
G
G
Di Stefano
S
S
Abalain
J H
JH
Floch
H H
HH
D013741:3-Oxo-5-alpha-Steroid 4-Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D037102:Lectins / Q000378:metabolism; D008297:Male; D011467:Prostate / Q000201:enzymology*; D013379:Substrate Specificity
D037102:Lectins; D013741:3-Oxo-5-alpha-Steroid 4-Dehydrogenase