PURIFICATION AND PROPERTIES OF NEUTRAL ALPHA-1,4 GLUCOSIDASE FROM HUMAN SEMINAL PLASMA

Following a preliminary fractionation of neutral .alpha.-glucosidase (EC 3.2.1.20) from human seminal plasma, it was shown by ion exchange chromatography, Sephadex G-200 filtration and adsorption chromatography that this .alpha.-glucosidase activity corresponded to 2 isoenzymes having the same ability to hydrolyze p-nitrophenyl-.alpha.-D-glucopyranoside. Both isoenzymes present a heat-stable fraction at 60.degree. C, require the presence of divalent cations in the incubation medium to demonstrate their glycolytic activity, and are inhibited by maltotriose and maltose.They have a MW of approximately 200,000 daltons and different sedimentation profiles on sucrose density gradient. This basic knowledge appears to be the prerequisite for further studies dealing with the importance of such isoenzymes as markers of epididymal function in male infertility.