Mannose Binding Lectins of Vicia tetrasperma Seed and Their Immunological Relationship to Other Legume Lectins of Similar Specificity

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概要

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• Mannose specific lectins of Vicia tetrasperma were purified by affinity chromatography with Sephadex G-100, and ion exchange chromatography. Chromatofocusing using PBE-94 gel was successfully employed to separate the major isolectins, lectin I and II. Both lectins had the same molecular weight of 78,000 and were tetramers composed of a uniform subunit with a molecular weight of 18,700. Amino acid compositions of these lectins were quite similar to each other, rich in aspartic acid (and/or asparagine) and hydroxyl amino acids, and lacking methionine and cysteine. Agar gel double diffusion using anti V. tetrasperma lectin antiserum revealed that lectins from V. cracca, Pisum sativum, and Lens culinaris, all of which have mannose binding properties, were antigenically identical. The antiserum reacted with the analogous lectins from V.faba, V. hirsuta, and V. angusttfolia, but formation of a spur in the diffusion assay showed that they were slightly different from V. tetrasperma lectin.

• 日本植物生理学会の論文

著者

• Kochibe Naohisa

  Department of Biology, Faculty of Education, Gunma University

関連論文

• Mannose Binding Lectins of Vicia tetrasperma Seed and Their Immunological Relationship to Other Legume Lectins of Similar Specificity
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