lectin purification
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2012 ◽  
Vol 168 (3) ◽  
pp. 580-591 ◽  
Author(s):  
Maria Inês Sucupira Maciel ◽  
Maria do Socorro de Mendonça Cavalcanti ◽  
Thiago Henrique Napoleão ◽  
Patrícia Maria Guedes Paiva ◽  
Maria Teresa Jansem de Almeida Catanho ◽  
...  

1996 ◽  
Vol 42 (6) ◽  
pp. 609-612 ◽  
Author(s):  
Bhagyashree Joshi ◽  
Jayant M. Khire ◽  
Hephzibah SivaRaman ◽  
M. Islam Khan

A lectin was isolated from culture filtrates of Xanthomonas campestris NCIM 5028, by a simple procedure of hydrophobic chromatography on phenyl-Sepharose after ammonium sulphate precipitation. The lectin was a heterodimer, with subunit molecular masses of 30 000 and 28 000. Gel filtration on S-300 column, calibrated with markers, showed its molecular mass to be approximately 70 000. Its isoelectric point was 7.2. The agglutination of the rabbit erythrocytes by the lectin was inhibited by fetuin glycopeptides and host plant (Brassica oleracea) extracts.Key words: Xanthomonas campestris, lectin, purification.


Nature ◽  
1974 ◽  
Vol 248 (5449) ◽  
pp. 599-600 ◽  
Author(s):  
R. W. REITHERMAN ◽  
S. D. ROSEN ◽  
S. H. BARONDES
Keyword(s):  

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