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Plant and Cell Physiology, 1986, Vol. 27, No. 4 661-669
© 1986

Article

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

Naohisa Kochibe

Department of Biology, Faculty of Education, Gunma University Aramaki, Maebashi 371, Japan

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. angustifolia, but formation of a spur in the diffusion assay showed that they were slightly different from V. tetrasperma lectin.

(Received December 24, 1985; Accepted March 12, 1986)
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