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Isolation of a Phosphoryl Choline-Binding Protein from the Hemolymph of the Snail, Achatina fulica

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Title Isolation of a Phosphoryl Choline-Binding Protein from the Hemolymph of the Snail, Achatina fulica
 
Creator Mandal, Chitra
Biswas, Margaret
Nagpurkar, Arun
Mookerjea, Sailen
 
Subject Cancer Biology and Inflammatory Disorder Division
 
Description 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.
 
Date 1991
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2289/1/DEVELOPMENTAL_AND_COMPARATIVE_IMMUNOLOGY__V._15___(_4__)227%2D239;1991.pdf
Mandal, Chitra and Biswas, Margaret and Nagpurkar, Arun and Mookerjea, Sailen (1991) Isolation of a Phosphoryl Choline-Binding Protein from the Hemolymph of the Snail, Achatina fulica. Developmental and Comparative Immunology, 15 (4). pp. 227-239.
 
Relation http://www.eprints.iicb.res.in/2289/