Purification and Quantification of Lactoferrin in Equine Seminal Plasma.

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  • INAGAKI Masami
    Laboratory of Biochemistry, School of Veterinary Medicine and Animal Sciences, Kitasato University
  • KIKUCHI Motohiro
    Laboratory of Theriogenology, School of Veterinary Medicine and Animal Sciences, Kitasato University
  • ORINO Koichi
    Laboratory of Biochemistry, School of Veterinary Medicine and Animal Sciences, Kitasato University
  • OHNAMI Yohji
    Laboratory of Theriogenology, School of Veterinary Medicine and Animal Sciences, Kitasato University
  • WATANABE Kiyotaka
    Laboratory of Biochemistry, School of Veterinary Medicine and Animal Sciences, Kitasato University

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Lactoferrin with a molecular mass of 80 kDa was purified from equine seminal plasma by heparin-Agarose affinity chromatography and Sephacryl S-200 gel filtration. Purified lactoferrin was found to be highly homogeneous on the bases of its migration as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and of the monospecificity of rabbit antibodies to the purified protein in immunoblotting of seminal plasma proteins. A sandwich enzyme-linked immunosorbent assay was developed for quantifying lactoferrin in equine seminal plasma. Seminal plasma lactoferrin concentrations in 23 normal stallions ranged from 42 to 453 μg/ml, with a mean value of 157 ± 118 μg/ml (S.D.).

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