Purification and spectral characterization of seminalplasmin, an antimicrobial protein from bull semen.

A new method for the purification of seminalplasmin, an antimicrobial protein from bull semen, was developed. The last step of the procedure involved preparative high performance liquid chromatography on a reversed phase column. Highly purified seminalplasmin was characterized by CD, absorption, fluorescence spectroscopy, double immunodiffusion and biological activity. Analytical ultracentrifugation revealed a molecular mass of 6300 Da. Amino-acid analysis of the protein preparation indicated the absence of sulfur-containing amino acids cysteine and methionine.