Deantigenation of human type B erythrocytes with Glycine max alpha-D-galactosidase.
Conversion of erythrocyte membrane B antigen to H antigen produces blood type O which is universally transfusable. If efficient large-scale production of enzymatically converted red blood cells is to be achieved, then optimal conditions for deantigenation must be determined. Cell suspension assays were used to study the blood group B activity of Glycine max (soybean) alpha-D-galactosidase on native human erythrocytes. The enzyme readily hydrolyzed the terminal alpha-D-galactosyl residue of the B antigen, converting it to H antigen. Optimal conditions for the enzymatic conversion of red cells with the Glycine enzyme are described. Normal cell morphology and function were maintained under optimal conditions.
Hobbs
L
L
Department of Pathology, University of Missouri, Columbia 65212, USA.
Mitra
M
M
Phillips
R
R
Haibach
H
H
Smith
D
D
D000017:ABO Blood-Group System / Q000276:immunology*; D000371:Agglutination; D000818:Animals; D001803:Blood Transfusion; D002417:Cattle; D006801:Humans; D007519:Isoantigens / Q000187:drug effects*; D013025:Glycine max / Q000201:enzymology*; D000519:alpha-Galactosidase / Q000494:pharmacology*
D000017:ABO Blood-Group System; D007519:Isoantigens; D000519:alpha-Galactosidase