The characterization of N-acetylglucosaminidases from the limpet Patella vulgata (L.) |
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Authors: | P.J.R. Phizackerley J.V. Bannister |
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Affiliation: | 1. The Nuffield Department of Clinical Biochemistry, Radcliffe Infirmary, Oxford OX2 6HE, U.K.;2. Department of Physiology and Biochemistry, Royal University of Malta, Msida, Malta |
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Abstract: | The α- and β-N-acetylglucosaminidase activity of the limpet Patella vulgata (L.) is due to two enzymes. One of these enzymes hydrolyses both α- and β-N-acetylglucosaminidases and is referred to α,β-N-acetylglucosaminidase. The other is a β-N-acetylglucosaminidase (EC 3.2.1.30). Both enzymes have been isolated and characterized as glycoproteins containing 12% hexose, mainly galactose. The amino acid, neutral sugar and amino sugar content of the two enzymes is very similar, and the main difference lies in the presence of 9% sialic acid in β-N-acetylglucosaminidase. The molecular weight of α,β-N-acetylglucosaminidase is 217 000 and that of β-N-acetylglucosaminidase is 136 000. Evidence has been obtained for the presence of an additional sub-unit in the α,β-enzyme. |
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Keywords: | Address for reprint requests: Dept of Physiology and Biochemistry Royal University of Malta Msida Malta |
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