Isolation and properties of a lectin from the seeds of Mimosa invisa L.
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Date
1987-12
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Abstract
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 ASepharose.
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.
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Keywords
Lectin, Mimosa invisa, Rhizobium
Citation
R Chandrika, Shaila M S. Isolation and properties of a lectin from the seeds of Mimosa invisa L. Journal of Biosciences. 1987 Dec; 12(4): 383-391.