Abstract
The red marine alga Ptilota plumosa has been shownto contain an anti-human blood group B lectin. We report here a new isolationprocedure by affinity chromatography on Sephadex G-200 and characterisation ofthe isolated lectin. The M r , determined by gelfiltration, was 52,500. SDS-PAGE revealed a single protein band withM r 17,440, indicating the native lectin was atrimer of subunits with the same Mr, as reported for the lectinsfromtwo other Ptilota species, P.filicinaand P. serrata. Analysis of amino acid composition showedslightly more basic than acidic amino acids. This was in contrast to theP. filicina and P. serrata lectinspreviously found to contain a higher proportion of acidic than basic aminoacids. Haemagglutination inhibition tests showed the P.plumosa lectin was inhibited by galactose, glucose and theirderivatives with p-nitrophenyl-α-D-galactoside moststrongly inhibitory. All glycoproteins tested failed to inhibit the lectin. Theamino acid composition, human blood group-B specificity and lack of inhibitionby glycoproteins indicate the lectin from P. plumosapossesses unique characteristics among marine algal lectins.
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Sampaio, A.H., Rogers, D.J., Barwell, C.J. et al. New affinity procedure for the isolation and further characterization of the blood group B specific lectin from the red marine alga Ptilota plumosa . Journal of Applied Phycology 14, 489–495 (2002). https://doi.org/10.1023/A:1022327010736
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DOI: https://doi.org/10.1023/A:1022327010736