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

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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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

Fingerprint

Galactosidases
Soybeans
Erythrocytes
Antigens
Erythrocyte Membrane
Enzymes
Blood Group Antigens
Population Groups
Glycine
Suspensions
H antigen

Keywords

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

ASJC Scopus subject areas

  • Pharmacology

Cite this

Deantigenation of human type B erythrocytes with Glycine max α-D-galactosidase. / Hobbs, L.; Mitra, M.; Phillips, R.; Haibach, H.; Smith, Daniel.

In: Biomedicine and Pharmacotherapy, Vol. 49, No. 5, 1995, p. 244-250.

Research output: Contribution to journalArticle

Hobbs, L. ; Mitra, M. ; Phillips, R. ; Haibach, H. ; Smith, Daniel. / Deantigenation of human type B erythrocytes with Glycine max α-D-galactosidase. In: Biomedicine and Pharmacotherapy. 1995 ; Vol. 49, No. 5. pp. 244-250.
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