Abstract
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 for-malinized 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.
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