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Biotechnology and Applied Biochemistry (2003) 37, (157–163) (Printed in Great Britain)

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

Hsin-Yeh Hsieh and Daniel Smith¹

Department of Pathology and Anatomical Sciences, University of Missouri-Columbia, M263 Medical Science Building, One Hospital Drive, Columbia, MO 65212, U.S.A.

Key words: ABO blood group, a-N-acetylgalactosaminidase, blood group A₂, Clostridium perfringens, universal red blood cells.

Abbreviations used: DTT, dithiothreitol; CPD, citrate/phosphate/dextrose; CPDA-1, citrate/phosphate/dextrose/adenine 1; AS-1, Adosl.

¹To whom correspondence should be addressed (e-mail SmithDS@health.missouri.edu).

Enzymic modification of type A₂ erythrocyte membranes with Clostridium perfringens a-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-a-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 a-N-acetylgalactosaminidase might be added directly to packed A₂ red-blood-cell units for enzymic conversion to blood type O. Further studies are warranted.

Received 27 August 2002/15 November 2002; accepted 18 November 2002

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