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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Purification and partial characterization of a N-glycolylneuraminic acid specific lectin from the clam Anadara granosa (L).

The N-glycolylneuraminic acid-specific lectin (AFL) from the foot muscles of the marine clam Anadara granosa has been purified to homogeneity by affinity chromatography on bovine submaxillary mucin-Sepharose 4B. The Ca(2+)-dependent lectin agglutinates rabbit erythrocytes. The purified lectin is a tetrameric protein of native M(r) 254 kDa having a pI value of 6.65. The M(r) of two subunits is 65 kDa each and that of the remaining two is 62 kDa each. The dominant amino acids of the lectin are aspartic acid, glutamic acid, serine and glycine. The lectin activity is inhibited only by N-glycolylneuraminic acid specially when it is present in the macromolecular structure of mucin viz., porcine submaxillary mucin, which is the most potent inhibitor. The binding site does not recognize N-acetylneuraminic acid. Due to this strict specificity, the lectin appears to be unique.[1]

References

  1. Purification and partial characterization of a N-glycolylneuraminic acid specific lectin from the clam Anadara granosa (L). Dam, T.K., Sarkar, M., Ghosal, J., Choudhury, A. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
 
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