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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002942:Circular Dichroism; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics; D005779:Immunodiffusion; D008297:Male; D008970:Molecular Weight; D011506:Proteins / Q000302:isolation & purification* / Q000633:toxicity; D012661:Semen / Q000032:analysis*; D029607:Seminal Vesicle Secretory Proteins; D014158:Transcription, Genetic / Q000187:drug effects
D000596:Amino Acids; D011506:Proteins; D029607:Seminal Vesicle Secretory Proteins