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International Journal of Zoology and Applied Biosciences Research Article

Identification and characterization of a naturally occurring agglutinin of the may beetle Phyllophaga sp.

C. Anitha, M.R. Basil-Rose and P.T. Arokya Glory

Year : 2018 | Volume: 3 | Issue: 2 | Pages: 157-162

doi: https://doi.org/10.5281/zenodo.1314014

Received on: 03/11/2018

Revised on: 04/04/2018

Accepted on: 04/06/2018

Published on: 04/07/2018

  • C. Anitha, M.R. Basil-Rose and P.T. Arokya Glory( 2018).

    Identification and characterization of a naturally occurring agglutinin of the may beetle Phyllophaga sp.

    . International Journal of Zoology and Applied Biosciences, 3( 2), 157-162.

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Abstract

A naturally occurring hemagglutinin with high affinity for rabbit erythrocytes was identified in the whole body extract of the May beetle Phyllophaga sp. The extract of the whole body also agglutinated pig, human A, human AB, rat, human B and O erythrocytes with diverse specificities. However, it failed to agglutinate cow, goat and buffalo erythrocytes. Physico-chemical analysis of the agglutinin using rabbit erythrocytes as indicator cells revealed that the agglutinin was at its highest activity between pH 7.5 to 8.5, temperature 35oC and in the presence of 10 mM Ca2+ in the buffer. Agglutinability of the whole body extract of the May beetle was slightly enhanced by low concentrations (0.01 to 5 mM) of disodium EDTA, unaffected by trisodium citrate (0.01 to 50 mM) and tetrasodium EDTA (0.01 to 1 mM). However, higher concentration of disodium EDTA (> 10 mM) greatly reduced the agglutinability than tetrasodium EDTA and trisodium citrate. Hemagglutinability inhibition assay recognized lactoferrin (HAI titer = 512) as the potent inhibitor of the agglutinin found in the whole body extract of the May beetle Phyllophaga sp. Presence of Ca2+ dependent natural agglutinin in the whole body extracts of the May beetle, Phyllophaga sp. may contribute to its defense mechanism.

Keywords

Agglutinins, Erythrocytes, Hemagglutination, Hemagglutination inhibition, Lectin, Phyllophaga sp.