title: Purification of human erythrocyte transglutaminase by immunoaffinity chromatography.
abstract: Human erythrocyte transglutaminase was purified using a reusable immunoaffinity column prepared from a monoclonal antibody described previously (Birckbichler et al., Hybridoma, 4, 179-186, 1985). The purified TGase was catalytically active and exhibited a single band of apparent Mr = 85,000 on SDS-PAGE and Western blotting. The amino acid composition of the enzyme was determined. The amino terminus was blocked, and the carboxy-terminal residue appeared to be isoleucine.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007118:Immunoassay; D008970:Molecular Weight; D011503:Transglutaminases / Q000097:blood* / Q000276:immunology
chemical_list: D000596:Amino Acids; D000911:Antibodies, Monoclonal; D011503:Transglutaminases