Purification and properties of human seminal maltase

Abstract

The maltase activity of human seminal plasma was studied by paper chromatographic and glucose oxidase methods and expressed in terms of the glucose liberated from the maltose substrate used. The specificity of maltase was established by selectively inhibiting the enzyme activity with tris buffer. Seminal maltase and amylase were separated and partially purified. Purified maltase preparation did not exhibit any amylase, maltose phosphorylase or transglucosidase activity. The maltase activity of semen is predominantly associated with seminal plasma and proceeds at maximal velocity at pH 6.0. The prostate gland seems to contribute most of the enzyme activity to the seminal plasma. The significance of the presence of maltase in seminal plasma and also in cervical mucus is discussed.