Clostridium perfringens α-N-acetylgalactosaminidase blood group A2-degrading activity

Hsin Yeh Hsieh, Daniel Smith

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Enzymic modification of type A2 erythrocyte membranes with Clostridium perfringens α-N-acetylgalactosaminidase was investigated. An ELISA demonstrated hydrolysis of type A2 epitopes under conditions of red-blood-cell collection and storage. The enzyme hydrolysed the terminal N-acetyl-α-D-galactosamine from the blood type A2 antigen, producing H antigen, blood group O, which is universally compatible in the ABO system. The enzyme was active in common red-cell preservative solutions at pH 6.4-7.0, at 4°C, at ionic strengths found in stored red cell units and in the presence of type A plasma. These data imply that the C. perfringens α-N-acetylgalactosaminidase might be added directly to packed A2 red-blood-cell units for enzymic conversion to blood type O. Further studies are warranted.

Original languageEnglish (US)
Pages (from-to)157-163
Number of pages7
JournalBiotechnology and Applied Biochemistry
Volume37
Issue number2
DOIs
StatePublished - Apr 1 2003

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Keywords

  • ABO blood group
  • Blood group A
  • Clostridium perfringens
  • Universal red blood cells
  • α-N-acetylgalactosaminidase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Molecular Medicine
  • Biomedical Engineering
  • Applied Microbiology and Biotechnology
  • Drug Discovery
  • Process Chemistry and Technology

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