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Updated: Jul 4, 2026

A Colorimetric Assay that Specifically Measures Granzyme B Proteolytic Activity: Hydrolysis of Boc-Ala-Ala-Asp-S-Bzl
Published on: November 28, 2014
Clostridium perfringens alpha-N-acetylgalactosaminidase blood group A2-degrading activity
1Department of Pathology and Anatomical Sciences, University of Missouri-Columbia, M263 Medical Science Building, One Hospital Drive, Columbia, MO 65212, U.S.A.
Abstract:
Enzymic modification of type A(2) erythrocyte membranes with Clostridium perfringens alpha-N-acetylgalactosaminidase was investigated. An ELISA demonstrated hydrolysis of type A(2) epitopes under conditions of red-blood-cell collection and storage. The enzyme hydrolysed the terminal N-acetyl-alpha-D-galactosamine from the blood type A(2) 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 degrees 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 alpha-N-acetylgalactosaminidase might be added directly to packed A(2) red-blood-cell units for enzymic conversion to blood type O. Further studies are warranted.
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