Purification and quantification of lactoferrin in equine seminal plasma.
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 microg/ml, with a mean value of 157 +/- 118 microg/ml (S.D.).
Inagaki
Masami
M
Laboratory of Biochemistry, School of Veterinary Medicine and Animal Sciences, Kitasato University, Towada, Aomori, Japan.
Kikuchi
Motohiro
M
Orino
Koichi
K
Ohnami
Yohji
Y
Watanabe
Kiyotaka
K
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006736:Horses / Q000378:metabolism*; D007781:Lactoferrin / Q000032:analysis / Q000302:isolation & purification*; D008297:Male; D008970:Molecular Weight; D012661:Semen / Q000378:metabolism*
D007781:Lactoferrin