Action of Proteases on Human Erythrocyte Glycoproteins in Relation to Hemagglutination by Conidiobolus Chitin-binding Agglutinin
スポンサーリンク
概要
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An extracellular proteolytic enzyme was produced by Conidiobolus lamprauges accompanied with chitin-binding hemagglutinin. The protease was partially purified by ammonium sulfate precipitation and CM Sephadex, concanavalin A-Sepharose, and Sephadex G-75 chromatographies. The molecular weight was estimated to be about 20, 000 by gel filtration. Agglutination of human erythrocytes by C. lamprauges agglutinin, wheat germ agglutinin, soy bean agglutinin and concanavaline A was accelerated by treating erythrocytes with this enzyme, whereas agglutination by Streptomyces L-fucose-specific lectin was not affected. Agglutination by Vibrio was repressed. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the erythrocyte membrane preparations from digested cells showed that this protease and pronase hydrolyzed "Band 3" and sialoglycoproteins [Fairbanks et al., Biochemistry, 10, 2606 (1971)] whereas papain and trypsin hydrolyzed only the latter. The relationships between these membrane proteins and the receptors for hemagglutinins were discussed.
- 社団法人 日本農芸化学会の論文
著者
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AIDA Ko
Institute of Applied Microbiology, The University of Tokyo
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Oishi Kunio
Institute Of Applied Microbiology The University Of Tokyo:(present Office)college Of Agriculture And
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Ishikawa Fumiyasu
Institute Of Applied Microbiology University Of Tokyo
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TAKENAKA Akio
Institute of Applied microbiology, The University of Tokyo
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KAMEYAMA Toshiyuki
Institute of Applied microbiology, The University of Tokyo
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