A novel lectin in rabbit serum binds H type 1, H type 2 and N-acetyl lactosamine structures

• Published in: Biochimica et Biophysica Acta (BBA) - General Subjects Vol. 1157; no. 1; pp. 45 - 49
• Main Authors: Hosomi, Osamu, Takeya, Akira, Yazawa, Shin
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 07.05.1993; Elsevier BV; Elsevier
• Subjects: Affinity chromatography; Amino Sugars; Amino Sugars - metabolism; Animals; Biological and medical sciences; Carbohydrate Sequence; Cells, Cultured; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Haptens; Haptens - classification; Haptens - metabolism; Hemagglutination Inhibition Tests; Hemagglutination reaction; Hemagglutination Tests; Humans; Immunohematology; Lectins; Lectins - blood; Lectins - isolation & purification; Lectins - metabolism; Molecular Sequence Data; Molecular Weight; Rabbit serum lectin; Rabbits; Red blood cell immunology; Synthetic oligosaccharides; PBS; SDS; RSL; PAGE; 3′-SLac; Hemagglutination reaction; GalNAc; Lac; BSA; LNF-II; Gal; LNF-I; Affinity chromatography; Fuc; Rabbit serum lectin; LacNac; 2′-FucLac; GlcNAc; Synthetic oligosaccharides; Glc; Human origin; Lectin; Hemagglutination inhibition test; Hemagglutination test; Red blood cell; O(H)-Blood group; Rabbit; Animal origin; Glycoproteins; Lagomorpha; Vertebrata; Mammalia; Binding capacity; Serum; H antigen
• DOI: 10.1016/0304-4165(93)90076-K
• ISSN: 0304-4165; 0006-3002

A novel lectin (RSL) which recognizes blood group H type 1 and type 2 (Fuc α1 → 2Gal β1 → 3/4GlcNAc β-R), and N-acetyllactosamine(Gal β1 → 4GlcNAc β-R) was purified from rabbit serum using affinity chromatography on Synsorb H type 2 beads, gel filtration and preparative polyacrylamide gel electrophoresis. The lectin agglutinated human O type red cells, and the hemagglutination reaction was inhibited by H type 1 and type 2 haptens, N-acetyllactosamine and human salivas from secretor individuals. The molecular weight of the lectin was estimated to be approxmate 650000 and 65000 on Sephacryl S-400 gel filtration and SDS-polycrylamidde gel electrophoresis, respectively.