Purification and some properties of chitin-binding hemagglutinin from Conidiobolus lamprauges.

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概要

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• A chitin-binding hemagglutinin was purified about 50-fold from the culture filtrate of Conidiobolus lamprauges. Hemolytic factor(s) and β-N-acetylglucosaminidase coexisting with the hemagglutinin were removed by treating the culture filtrate with CM Sephadex and formalinized human erythrocytes. Purified hemagglutinin formed large aggregates upon ultrafiltration. The hemagglutinin had a major and a minor band in sodium dodecyl sulfate polyacrylamide gel electrophoresis. The major band of this hemagglutinin was a protein containing a small amount of sugar, and its molecular weight was approximately 86, 000. The hemagglutinin was strongly inhibited by N-acetyl chitobi, tri and tetraose; moderately inhibited by phenyl and p-nitrophenyl β-N-acetyl-D-glucosaminides; and weakly inhibited by D-glucosamine and N-acetyl-D-glucosamine. β-Configuration was required for inhibition.

• 公益社団法人 日本農芸化学会の論文

著者

• OISHI Kunio

  Institute of Applied Microbiology, The University of Tokyo

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• Purification and some properties of chitin-binding hemagglutinin from Conidiobolus lamprauges.

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