Abstract
The activity of purified preparation of decapacitation factor (DF), an antifertility factor present in mammalian seminal plasma, was destroyed by proteolytic enzymes indicating that DF contains essential peptide bonds. Chemical tests on the DF preparation revealed the presence of histidine and arginine and gave color with ninhydrin and chlorine-tolidine typical of peptides. Specific hydrolyses indicated absence of an ester bond and possible presence of an amide or aspartyl peptide bond necessary for activity. The DF preparation was purified from 3 l of bull seminal plasma approximately 1000-fold by ultracentrifugation, water extraction of the sediment, Pronase digestion, dialysis and column chromatography on Sephadex G-10 and powdered cellulose.
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