Glycosylated human prolactin.
A glycosylated form of human PRL (G-hPRL) was isolated from pituitary glands. The glycoprotein was separated from the major form of PRL on columns of lentil lectin-Sepharose 4B. The major form of PRL did not bind to the lentil lectin, whereas the glycosylated modification did and could be eluted with methyl-alpha-D-mannopyranoside. By gel electrophoresis in sodium dodecyl sulfate, a mol wt of 25,000 was estimated for the glycosylated PRL. The mol wt of hPRL is 23,000. In a RIA for hPRL, the glycosylated hormone was about one third as reactive as the principal form. Since there is only one Asn-X-Ser(Thr) sequence in hPRL, the asparagine at position 31 is the likely point of N-linked glycosylation.
Lewis
U J
UJ
Singh
R N
RN
Sinha
Y N
YN
Vanderlaan
W P
WP
D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000276:immunology; D006801:Humans; D007158:Immunologic Techniques; D008970:Molecular Weight; D010902:Pituitary Gland / Q000032:analysis*; D011388:Prolactin / Q000031:analogs & derivatives* / Q000276:immunology / Q000302:isolation & purification; D011863:Radioimmunoassay; D013194:Staining and Labeling
D000939:Epitopes; C043928:prolactin, glycosylated; D011388:Prolactin