Production, Purification, and Characterization of Neurospora sitophila Lectin(Microbiology & Fermentation Industry)

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概要

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• Neurospora sitophila produced extracellular and cell wall-associated lectins. The addition of L-sorbose to a culture resulted in a decrease in the production of the former lectin and complete abolition of the latter. The lectin in the culture filtrate was purified by bovine submaxillary mucin-conjugated Sepharose chromatography. The molecular weight of the lectin was calculated to be approx. 40,000 by Sephacryl S-200 gel filtration, and that of the subunit to be approx. 22,000 by SDS/polyacrylamide-gel electrophoresis. The lectin was not inhibited by simple sugars or their homopolymers. It was inhibited strongly by glycoproteins from human erythrocyte membrane and bovine submaxillary mucin, and moderately by α1-acid glycoprotein from human plasma, human IgA and IgM, and fetal calf fetuin. The lectin agglutinated human type A, B and O erythrocytes to the same degree. Erythrocytes from chick, horse, rabbit and sheep were more efficiently agglutinated.

• 社団法人日本農芸化学会の論文
• 1989-07-23

著者

• OISHI Kunio

  Institute of Applied Microbiology, The University of Tokyo

• Oishi Kunio

  Institute Of Applied Microbiology The University Of Tokyo:(present Office)college Of Agriculture And

• Oishi Kunio

  Institute Of Applied Microbiology University Of Tokyo

• ISHIKAWA Fumiyasu

  Institute of Applied Microbiology, University of Tokyo

• Ishikawa Fumiyasu

  Institute Of Applied Microbiology University Of Tokyo

関連論文

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• Production, Purification, and Characterization of Neurospora sitophila Lectin(Microbiology & Fermentation Industry)
• Inhibition of Restriction Endonucleases by Commercial Polysaccharides
• Action of Proteases on Human Erythrocyte Glycoproteins in Relation to Hemagglutination by Conidiobolus Chitin-binding Agglutinin
• Distribution of Highly Specific Arylamidase Activities in Bacteria
• Purification and Immunological Properties of Chitin-binding Hemagglutinin and β-N-Acetylglucosaminidase Produced by Conidiobolus lamprauges
• Purification and Properties of a New L-Fucose-specific Lectin Produced by Streptomyces No. 100-2
• Purification and some properties of chitin-binding hemagglutinin from Conidiobolus lamprauges.

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