A T-antigen-binding lectin from Channa leucopunctatus (Murrel) plasma.
The plasma of Channa leucopunctatus, which agglutinates human A,B,O blood-group erythrocytes nonspecifically, contains three separate agglutinating activities that are distinguishable by hemagglutination with specific blood-group erythrocytes. Blood group A agglutinating activity of the plasma was separated from the other two hemagglutinating activities by DEAE-cellulose column chromatography and further purified to homogeneity by affinity chromatography on 2-acetamido-2-deoxy-D-galactose coupled to epoxy-activated Sepharose 6B. The apparent homogeneity of the lectin was established by poly(acrylamide) gel electrophoresis, isoelectric focusing, immunodiffusion, and cross-immunoelectrophoresis. The native protein has a mol. wt. of 140,000 and two identical subunits. The isoelectric point of the affinity-purified lectin is 4.6. Amino acid analysis indicated high proportions of glycine, alanine, and aspartic acid. The lectin is a glycoprotein and it has a requirement for divalent cations, Ca2+ and Mg2+ or Mn2+, for hemagglutinating activity. 2-Acetamido-2-deoxy-D-galactose, 4-nitrophenyl 2-acetamido-2-deoxy-alpha-D-galactopyranoside, T-antigenic disaccharide, and Forssman glycolipid are potent inhibitors.
C.S.I.R. Centre for Biochemicals, Delhi University Campus, India.
S R
SR
Manihar
R H
RH
Das
H R
HR
Das
D000017:ABO Blood-Group System; D000818:Animals; D000957:Antigens, Viral, Tumor / Q000378:metabolism*; D002240:Carbohydrate Sequence; D005399:Fishes / Q000097:blood*; D006385:Hemagglutination Inhibition Tests; D006388:Hemagglutinins / Q000097:blood; D006801:Humans; D066298:In Vitro Techniques; D037102:Lectins / Q000097:blood*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry / Q000494:pharmacology
D000017:ABO Blood-Group System; D000957:Antigens, Viral, Tumor; D006388:Hemagglutinins; D037102:Lectins; D009844:Oligosaccharides