Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin |
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| Authors: | Fumio Yagi Mariko Miyamoto Tamami Abe Yuji Minami Kenjiro Tadera Irwin J Goldstein |
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| Affiliation: | (1) Biochemistry and Biotechnology, Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima 890, Japan;(2) Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA |
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| Abstract: | A lectin was isolated from fruiting bodies of Agrocybe cylindracea by two ion-exchange chromatographies and gel filtration on Toyopearl HW55F. The lectin was homogeneous on polyacrylamide gel electrophoresis and its molecular mass was determined to be 30 000 by gel filtration, and 15 000 by sodium dodecylsulfate polyacrylamide gel electrophoresis, signifying a dimeric protein. Its carbohydrate-binding specificity was investigated both by sugar-hapten inhibition of hemagglutination and by enzyme-linked immunosorbent assay. The inhibition tests showed the affinity of the lectin to be weakly directed toward sialic acid and lactose, and the enhanced affinity toward trisaccharides containing the NeuAcα2,3Galβ-structure. Importantly, the lectin strongly interacted with glycoconjugates containing NeuAcα2,3Galβ1,3GlcNAc-/GalNAc sequences. This revised version was published online in November 2006 with corrections to the Cover Date. |
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| Keywords: | Agrocybe cylindracea fungal lectin carbohydrate-binding specificity sialic acid-containing carbohydrate chain |
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