Deantigenation of human type B erythrocytes with Glycine max α-D-galactosidase

L. Hobbs, M. Mitra, R. Phillips, H. Haibach, D. Smith

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

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) α-D-galactosidase on native human erythrocytes. The enzyme readily hydrolyzed the terminal α-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.

Original languageEnglish (US)
Pages (from-to)244-250
Number of pages7
JournalBiomedicine and Pharmacotherapy
Volume49
Issue number5
DOIs
StatePublished - 1995
Externally publishedYes

Keywords

  • blood group B
  • transfusion
  • α-D-galactosidase

ASJC Scopus subject areas

  • Pharmacology

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