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

Hsin Yeh Hsieh, Daniel Smith

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 2003
Externally publishedYes

Fingerprint

Clostridium
Clostridium perfringens
Blood Group Antigens
varespladib methyl
Blood
Antigens
Erythrocytes
ABO Blood-Group System
Acetylgalactosamine
Galactosamine
Enzymes
Food preservatives
Erythrocyte Membrane
Epitopes
Ionic strength
Osmolar Concentration
Hydrolysis
Enzyme-Linked Immunosorbent Assay
Cells
Membranes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology

Cite this

Clostridium perfringens α-N-acetylgalactosaminidase blood group A2-degrading activity. / Hsieh, Hsin Yeh; Smith, Daniel.

In: Biotechnology and Applied Biochemistry, Vol. 37, No. 2, 04.2003, p. 157-163.

Research output: Contribution to journalArticle

@article{6f6a29f841f14a4e80009e891e2123f5,
title = "Clostridium perfringens α-N-acetylgalactosaminidase blood group A2-degrading activity",
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.",
keywords = "α-N-acetylgalactosaminidase, ABO blood group, Blood group A, Clostridium perfringens, Universal red blood cells",
author = "Hsieh, {Hsin Yeh} and Daniel Smith",
year = "2003",
month = "4",
doi = "10.1042/BA20020073",
language = "English (US)",
volume = "37",
pages = "157--163",
journal = "Biotechnology and Applied Biochemistry",
issn = "0885-4513",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Clostridium perfringens α-N-acetylgalactosaminidase blood group A2-degrading activity

AU - Hsieh, Hsin Yeh

AU - Smith, Daniel

PY - 2003/4

Y1 - 2003/4

N2 - 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.

AB - 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.

KW - α-N-acetylgalactosaminidase

KW - ABO blood group

KW - Blood group A

KW - Clostridium perfringens

KW - Universal red blood cells

UR - http://www.scopus.com/inward/record.url?scp=0037384867&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037384867&partnerID=8YFLogxK

U2 - 10.1042/BA20020073

DO - 10.1042/BA20020073

M3 - Article

VL - 37

SP - 157

EP - 163

JO - Biotechnology and Applied Biochemistry

JF - Biotechnology and Applied Biochemistry

SN - 0885-4513

IS - 2

ER -