Purification and partial biochemical characterization of an S-type lectin from blastula embryos of Bufo arenarum.
1. S-type lectin from Bufo arenarum embryos at blastula stage was purified by affinity chromatography. The molecule is a dimer with equal-sized monomers and the apparent subunit molecular weight was found to be 14.5 kDa. 2. Analytical isoelectric focusing of the pure lectin showed an acidic pI of 4.7. 3. Inhibition of the hemagglutination by mono- and oligosaccharides revealed a specificity for sugars bearing a beta-galactoside configuration. 4. Crossreactivity studies between the blastula lectin and the one purified earlier from adult ovary performed by immunodotting, ELISA and immunoblotting showed that these lectins share many epitopes.
Elola
M T
MT
Departamento de Ciencias Biológicas, Universidad Nacional de La Plata, Argentina.
Fink
N E
NE
D000818:Animals; D001755:Blastocyst / Q000737:chemistry*; D002022:Bufo arenarum / Q000378:metabolism*; D002846:Chromatography, Affinity; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000737:chemistry; D005260:Female; D006385:Hemagglutination Inhibition Tests; D007120:Immunochemistry; D007526:Isoelectric Point; D037102:Lectins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D008297:Male; D008970:Molecular Weight; D010053:Ovary / Q000737:chemistry
D000939:Epitopes; D037102:Lectins