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Isolation of a phosphoryl choline-binding protein from the hemolymph of the snail, Achatina fulica

Mandal, Chitra and Biswas, Margaret and Nagpurkar, Arun and Mookerje, Sailen (1991) Isolation of a phosphoryl choline-binding protein from the hemolymph of the snail, Achatina fulica. In: Developmental & Comparative Immunology, 15 (4). pp. 227-239.

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Official URL: http://dx.doi.org/10.1016/0145-305X(91)90016-R


A phosphorylcholine-binding protein from the hemolymph of the snail Achatina fulica was purified to near homogeneity using a Sepharose phenylphosphorylcholine affinity column. The protein bound to the affinity column was eluted with 5 mM phosphorylcholine as a single symmetrical peak. The purified protein (400 Kda) contained 35–40% carbohydrate. On SDS-PAGE the protein separated into two bands of 20 and 24 Kda, and had a pI of 5.9. On immunodiffusion, antiserum to the snail phosphorylcholine binding protein did not cross-react against other phosphorylcholine binding proteins, like rat serum phosphorylcholine-binding protein (PCBP), limulus C-reactive protein (CRP), or human CRP. On pretreatment of the snail hemolymph with this antiserum, the hemagglutination titer of the hemolymph was markedly decreased. The purified snail phosphorylcholine binding protein agglutinated rabbit erythrocytes in the absence of divalent cation (Ca+2) but trace amount of Ca+2 increased its binding. The strongest inhibitor of the agglutination reaction was lactose, followed by melibiose and 2-deoxygalactose. The relationships of the snail phosphorylcholine binding protein to other hemolymph agglutinins and to CRPs are discussed in light of common phylogeny.

Item Type: Journal Article
Publication: Developmental & Comparative Immunology
Publisher: Elsevier science
Additional Information: Copyright of this article belongs to Elsevier science.
Keywords: Phosphorylcholine;Phosphorylcholine-binding protein; C-reactive protein;Agglutinin;Achatina fulica,snail;Hemolymph.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 24 Nov 2010 06:59
Last Modified: 24 Nov 2010 06:59
URI: http://eprints.iisc.ac.in/id/eprint/33920

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