The heparin-binding activity of bull seminal plasma proteins was inhibited
by D-fructose, D-glucose, inulin and glycogen; D-galactose, dextran and man
nan had no effect. While the, ejaculated sperm-heparin interaction was not
influenced by the presence of saccharides, the heparin-binding activity of
epididymal sperm was inhibited by D-fructose. The results of the binding st
udies were confirmed by affinity chromatography on immobilized heparin foll
owed by elution with monosaccharides. Proteins adsorbed to a heparin-polyac
rylamide column and eluted with D-fructose were analyzed by RP RPLC, SDS el
ectrophoresis and by determination of the N-terminal amino-acid sequence. R
NAase dimer, PDC-109 and metalloproteinase inhibitor (TIMP-2) were identifi
ed.