Purification and characterization of N-acetyl-α-D-galactosaminidase from Gallus domesticus

J. Hata, M. Dhar, M. Mitra, M. Harmata, F. Haibach, P. Sun, D. Smith

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21 Scopus citations

Abstract

Exoglycosidases modify carbohydrate epitopes on glycoproteins and glycolipids. The N-acetyl-α-D-galactosaminidase from the domestic chicken, Gallus domesticus, is an important exoglycosidase which degrades the human blood group A epitope. This enzyme has never been demonstrably purified or thoroughly characterized. We have developed a technique to purify this enzyme to homogeneity. The isolated enzyme has a molecular weight of 49.1 kDa by SDS PAGE and 145.0 kDa by gel filtration. The enzyme is highly selective for PNP-N-acetyl-α-D-galactosaminide and is inactive against other low molecular weight substrates. The enzyme hydrolyzes the terminal N-acetyl-α- D-galactosaminide residues from blood group A2 erythrocytes. Protease activity is below detectable limits. The enzyme has a pH optima of 3.7, a pI of 8.15, is relatively unaffected by ionic strength, and is stable at 4°C.

Original languageEnglish (US)
Pages (from-to)77-86
Number of pages10
JournalBiochemistry International
Volume28
Issue number1
StatePublished - Jan 1 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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    Hata, J., Dhar, M., Mitra, M., Harmata, M., Haibach, F., Sun, P., & Smith, D. (1992). Purification and characterization of N-acetyl-α-D-galactosaminidase from Gallus domesticus. Biochemistry International, 28(1), 77-86.