Purification and properties of neutral α-1,4 glucosidase from human seminal plasma

Abstract

Following a preliminary fractionation of neutral α-glucosidase (E.C. 3.2.1.20) from human seminal plasma, we have shown by ion exchange chromatography, Sephadex G-200 filtration, and adsorption chromatography that this α-glucosidase activity corresponded to two iso-enzymes having the same ability to hydrolyse p-nitrophenyl-α-d-glucopyranoside. Both iso-enzymes present a heat-stable fraction at 60°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 molecular weight 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.

Key Words:

• α-1,4 glucosidase
• Human seminal plasma