XXXX and @entity2041 peroxidase in seminal plasma of @entity1 and bulls.

@entity1 @entity4259 @entity26 @entity2041 @entity2197 @entity291 @entity6743
High levels of @entity4259 and @entity2041 peroxidase ( @entity2197 -Px) were found in bull seminal plasma but low concentrations in @entity1 seminal plasma. In @entity1 the seminal plasma @entity4259 was associated with two macromolecules separable by gel filtration, but no @entity2197 -Px was found in the same fractions. @entity4259 in bull seminal plasma was associated with two proteins, which could be separated by gel filtration and anion exchange chromatography. Both macromolecules coeluted with @entity2197 -Px activity and had identical optima at pH 7.0. Their responses to thermal treatment, however, differed. Seminal vesicle secretory fluid in the bull contained both these proteins, while the larger molecule was also found in fractionations of ampulla, prostate and Cowper's glands. The larger enzyme form is evidently a tetramer of the smaller one. Both enzyme forms were extremely sensitive to heavy metals and some divalent metal ions. @entity2197 caused an activation while other reducing agents were suppressive. Triton X-100 had no effect, while @entity6743 was inhibitory. These properties are typical for a phospholipid hydroperoxide @entity2197 -Px. It is concluded that this @entity4259 -dependent enzyme may be important in the protection of @entity291 spermatozoa against damage caused by @entity26 radicals, while in @entity1 such a mechanism is not functional.
