Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide.
A glycosaminoglycan-bearing polypeptide (S.GP), present in human seminal plasma, was purified to homogeneity by a combination of CsCl density-gradient centrifugation, f.p.l.c. ion-exchange chromatography on a Mono Q HR column and Superose 6 gel filtration. The observed polydispersity of S.GP was attributed to the heterogeneity of its glycosaminoglycan content. Enzymic deglycosylation experiments and N-terminal amino-acid sequence determination indicate that it consists of a polypeptide (apparent molecular mass approx. 18 kDa) bearing both chondroitin and heparan sulphate chains. Evidence is given that S.GP contains a glycosaminoglycan-linkage domain of a so far uncharacterized gene product, proteolytically processed in the genital tract.
Bonnet
F
F
Laboratoire des Protéines, URA C.N.R.S. No. 1188, Université de Paris V, France.
Perin
J P
JP
Maillet
P
P
Jolles
P
P
Alliel
P M
PM
D000595:Amino Acid Sequence; D006025:Glycosaminoglycans / Q000737:chemistry*; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D011509:Proteoglycans / Q000737:chemistry*; D012661:Semen / Q000737:chemistry*; D014758:Viral Core Proteins / Q000737:chemistry
D006025:Glycosaminoglycans; D011509:Proteoglycans; D014758:Viral Core Proteins