Abstract
Soluble antigens, enzyme-linked immunosorbent assays (ELISA), and cell suspension assays were used to study the blood group B activity of Glycine max (soybean) α- d-galactosidase. The enzyme readily hydrolyzed the terminal α- d-galactosyl of the B antigen under a variety of conditions, converting it to H antigen. Conversion of the B antigen to H antigen produces blood type O which is universally transfusable. These preliminary studies are important in determining optimal conditions for enzymatic conversion of blood type B to O erythrocytes if efficient large-scale production of enzymatically converted, universally transfusable red blood cells is to be achieved.
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