Record Details

Purification and characterization of an extracellular agglutinin from Tricophyton rubrum with specificity towards sialic acid containing glycoconjugates

NOPR - NISCAIR Online Periodicals Repository

View Archive Info
 
 
Field Value
 
Title Purification and characterization of an extracellular agglutinin from Tricophyton rubrum with specificity towards sialic acid containing glycoconjugates
 
Creator Bhowal, J
Mitra, A
Banerjee, S
Sikdar, S
Guha, A K
Chatterjee, B P
 
Subject Tricophyton rubrum
Dermatophyte
Agglutinin
Glycoproteins
Hemagglutination
 
Description 81-88
An agglutinin, a monomeric glycoprotein with a molecular mass of about 6.5 kDa and containing 18% sugar has been purified to an apparent homogeneity from a 21 days old culture filtrate of an anthropophilic dermatophyte Tricophyton rubrum. It is a human blood group non-specific agglutinin which also agglutinates animal erythrocytes and Ehrlich ascites carcinoma and Sarcoma-180 cells. It is thermally stable and exhibits maximum activity at pH 8. Amino acid analysis shows a significant amount of glycine, with no cysteine. Glycoproteins inhibited the hemagglutination of the agglutinin, but not the simple sugars, including sialic acid. Fetuin is the most potent inhibitor among the glycoproteins tested. This inhibition gives a hint to binding with Gal β1-3GalNAc or Gal β1-4GlcNAc residue containing sialic acid at the terminal position with α 2-6 or α 2-3 linkage.
 
Date 2009-03-31T10:47:37Z
2009-03-31T10:47:37Z
2004-04
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/3643
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol. 41(2 & 3) [April-June 2004]