Calcium binding constituents of the organic shell matrix from the freshwater snail Biomphalaria glabrata

Comp Biochem Physiol B Biochem Mol Biol. 2000 Oct;127(2):235-42. doi: 10.1016/s0305-0491(00)00261-3.

Abstract

The Ca2+ binding of an EDTA-free water-soluble (SM) and -insoluble (IM) organic matrix of the freshwater snail Biomphalaria glabrata was investigated, using a 45Ca2+ autoradiography after SDS-electrophoretical separation and a calcium binding assay. Electrophoresis of the SM showed a considerable amount of Alcian blue and Stains all positive material, regarded as glycosaminoglycans (GAGs) or proteoglycans (PGs). This part of the SM was slightly positive after 45Ca2+ autoradiography at pH 6.8. The Ca2+ binding increased, raising the pH to 7.4 and 8.0 and was especially strong when simulating the real conditions of the extrapallial space with a carbonate buffer of pH 7.4. The Ca2+ binding assay of the IM showed the same pH-dependency that was observed in the SM. The titration of the IM with Ca2+ at pH 8.0 lead to a dissociation constant of 7.5 x 10(-5) M. While Mg2+ displaced 45Ca2+ in the same way as nonradioactive Ca2+, an approximately 400-fold amount of Na+ was necessary to reduce the binding of 45Ca2+ to 50%. The Ca2+ binding of the organic matrix from the B. glabrata shell appears to be a process of low specificity, medium affinity and high pH-dependency. Apparently, acidic carbohydrate-rich PGs are the only calcium binding constituents of the organic shell matrix.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Autoradiography
  • Calcium / metabolism*
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Glycosaminoglycans / chemistry
  • Glycosaminoglycans / metabolism
  • Hydrogen-Ion Concentration
  • Protein Binding
  • Proteoglycans / chemistry
  • Proteoglycans / metabolism
  • Snails / chemistry*
  • Snails / metabolism*

Substances

  • Glycosaminoglycans
  • Proteoglycans
  • Calcium