Endo‐β‐Galactosidases and Keratanase

Michiko N. Fukuda1

1 La Jolla Cancer Research, La Jolla, California
Publication Name:  Current Protocols in Molecular Biology
Unit Number:  Unit 17.17B
DOI:  10.1002/0471142727.mb1717bs32
Online Posting Date:  May, 2001
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Abstract

This overview covers the endo‐β‐galactosidases; enzyme is capable of hydrolyzing a wide range of glycoconjugates. Endo‐β‐galactosidases from numerous sources are discussed in terms of their substrate specificities and substrates, as well as their practical research applications.

     
 
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Table of Contents

  • Introduction
  • Endo‐β‐Galactosidase from E. Freundii
  • Literature Cited
  • Figures
     
 
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Materials

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Figures

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Literature Cited

Literature Cited
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   Fukuda, M.N. 1985. Isolation and characterization of a new endo‐β‐galactosidase from Diplococcus pneumoniae. Biochemistry 24:2154‐2163.
   Fukuda, M.N. and Matsumura, G. 1975. Endo‐β‐galactosidase of Escherichia freundii. Hydrolysis of pig colonic mucin and milk oligosaccharides by endoglycosidic action. Biochem. Biophys. Res. Commun. 64:465‐471.
   Fukuda, M.N. and Matsumura, G. 1976. Endo‐β‐galactosidase of Escherichia freundii. Purification and endoglycosidic action on keratansulfates, oligosaccharides and blood group active glycoprotein. J. Biol. Chem. 251:6218‐6225.
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