Inhibition of acrosine-like protease activity by a lectin affinity chromatographic bovine seminal plasma fraction containing the PDC-109 and aSFP proteins.
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.
Marquínez
A C
AC
Centro de Investigaciones en Reproducción, Facultad de Medicina, Paraguay, Buenos Aires, Argentina.
Andreetta
A M
AM
Chen
J S
JS
Menesini Chen
M G
MG
Wolfenstein Todel
C
C
Scacciati de Cerezo
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity / Q000379:methods*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry; D008297:Male; D011480:Protease Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D012661:Semen / Q000737:chemistry*; D029589:Seminal Plasma Proteins
D037102:Lectins; D011480:Protease Inhibitors; D011506:Proteins; D029589:Seminal Plasma Proteins; C425042:spermadhesin; D010450:Endopeptidases