Effect of purification of bovine serum albumin on the interaction of human semen with mouse ova in vitro.

Abstract

Mouse ova degenerate in medium containing untreated bovine serum albumin (BSA) when incubated for 18—24h with highly motile human spermatozoa not completely freed from a seminal plasma component. The human seminal plasma component also has a detrimental effect on the motility of human spermatozoa in the presence of untreated BSA, but both mouse ova and human spermatozoa are unaffected by human seminal plasma when the culture medium contains purified BSA as a protein source. The active component from human seminal plasma is most probably spermine. This polyamine reacts with the untreated BSA with a component that is pronase sensitive, heat labile and only partially dialyzable. The BSA component is not precipitated by trichloroacetic acid but is soluble in ethanol. Although the nature of the seminal plasma-BSAinteraction suggests that the effect of BSA may be due to amine oxidase activity, attempts to assay endogenous amine oxidase activity in the untreated BSA have failed to detect it.