Inhibition of acrosine-like protease activity by a lectin affinity chromatographic bovine seminal plasma fraction containing the PDC-109 and aSFP proteins

J Chromatogr B Biomed Sci Appl. 2000 Sep 15;746(2):141-50. doi: 10.1016/s0378-4347(00)00308-x.

Abstract

These studies showed that the fractionation of bovine seminal plasma based on lectin agarose affinity chromatography, employing lectins specific to asparagine linked oligosaccharides, and a lectin specific for fucosylated glycans, lead to products with an inhibitory effect on the acrosine-like protease activity. This effect decreases when glycocompounds containing fucosylated Lewis(x) structures are removed, suggesting that these compounds might have some role in the modulation of this activity in the bull. In the fraction devoid of high mannose, hybrid and non-bisecting lactosaminic oligosaccharide-containing glycocompounds, PDC-109 and aSFP proteins were detected and characterized at microscale.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, Affinity / methods*
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Endopeptidases / chemistry
  • Endopeptidases / metabolism*
  • Lectins / chemistry
  • Male
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / pharmacology*
  • Proteins / analysis*
  • Proteins / chemistry*
  • Semen / chemistry*
  • Seminal Plasma Proteins

Substances

  • Lectins
  • Protease Inhibitors
  • Proteins
  • Seminal Plasma Proteins
  • spermadhesin
  • Endopeptidases