Altered glycosylation of gamma-glutamyltranspeptidase (GGT) in seminal fluid from men with accessory gland infection.
The heterogeneity of gamma-glutamyltranspeptidase (GGT) in seminal plasma has been studied using Con A-chromatography. This parameter was then related to the fructose concentration, the acid phosphatase activity, ejaculate volume, sperm density and the number of bacteria per ml. Multivariate regression analysis and stepwise elimination of the least fitting factors, revealed that Con A-binding correlated with the number of bacteria per ml of semen and the acid phosphatase activity with 49% of the variance of GGT-binding being explained by these parameters. This result suggests that glycosylation of seminal GGT is altered by accessory gland infection. Neuraminidase digestion suggests that the pattern of Con A-binding of seminal GGT depends only partly on its sialic acid content.
Delanghe
J
J
Comhaire
F
F
de Buyzere
M
M
Vermeulen
L
L
D000135:Acid Phosphatase / Q000032:analysis; D050260:Carbohydrate Metabolism; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000378:metabolism; D005832:Genital Diseases, Male / Q000201:enzymology*; D006801:Humans; D007239:Infections / Q000201:enzymology*; D008297:Male; D009439:Neuraminidase / Q000378:metabolism; D011472:Prostatitis / Q000201:enzymology; D012661:Semen / Q000201:enzymology*; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D003208:Concanavalin A; D005723:gamma-Glutamyltransferase; D000135:Acid Phosphatase; D009439:Neuraminidase