Chandrika, R and Shaila, MS (1987) Isolation and properties of a lectin from the seeds of Mimosa invisa L. In: Journal of Biosciences, 12 (4). pp. 383-391.
A lectin has been purified from the seeds of Mimosa 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-nodulating Rhizobium and is a panagglutinin; the agglutination is not inhibited by several simple sugars. It is thermo-stable and has no metal ions.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Indian Academy of Sciences.|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||09 Apr 2008|
|Last Modified:||19 Sep 2010 04:44|
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