Isolation and properties of a lectin from the seeds ofMimosa invisa L. |
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Authors: | R. Chandrika M. S. Shaila |
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Affiliation: | (1) Microbiology and Cell Biology Laboratory, Indian Institute of Science, 560 012 Bangalore, India;(2) Present address: Department of Urology, College of Physicians and Surgeons, Columbia University, 10032 New York, New York, USA |
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Abstract: | A lectin has been purified from the seeds ofMimosa invisa L. by gel filtration and preparative Polyacrylamide gel electrophoresis. The purified lectin was homogeneous as judged by analytical Polyacrylamide gel electrophoresis, immunodiffusion and Immunoelectrophoresis. The apparent molecular weight is 100,000; the protein is a tetramer with two types of subunits (molecular weight 35,000 and 15,000). The lectin is a glycoprotein with approximately 21% carbohydrate and interacts with Sephadex and concanavalin A-Sepharose. It agglutinates erthrocytes non-specifically, does not agglutinate leucocytes and is not mitogenic, agglutinates Mimosa-nodulatingRhizobium and is a panagglutinin; the agglutination is not inhibited by several simple sugars. It is thermo-stable and has no metal ions. |
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Keywords: | Lectin Mimosa invisa Rhizobium |
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