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Reprod Biol. 2009 Jul;9(2):151-60.

Purification and partial characterization of proteinase inhibitors of equine seminal plasma.

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  • 1Institute of Veterinary José Caetano Borges,, University of Uberaba, Uberaba, Minas Gerais, Av. Tutunas 720, Postal code 38061-500, Brazil.


The aims of the study were: 1/ to isolate and identify equine seminal plasma proteinase inhibitors, 2/ to evaluate their inhibitory potential, and 3/ to test a correlation between protein concentration in seminal plasma supernatant (obtained after precipitation with 36% ammonium sulfate) and stallion sexual maturity. Seminal plasma proteins obtained from six stallions were chromatographed in a Superose 12 (FPLC system) column followed by C(18) HPLC reverse-phase. Inhibition of trypsin amidase activity was evaluated in the collected fractions. Active proteins with a molecular mass of 6.3-7.0 KDa were identified using mass spectrometry. The older stallions showed a reduction in total seminal plasma protein concentration, but had similar concentrations of proteinase inhibitors (0.28+/-0.10 mg/ml) in seminal plasma supernatant. Different proteinase inhibitor isoforms were found in semen of all stallions which suggests that the isoforms may be used as biomarkers of individual animals.

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