Fig 1.
Location of the sampling site in the Saône River.
Site is shown by the arrow (↖: 47° 08’ 82.5”N, 05° 24’ 08.5”E; ◉: 47° 07’ 36.4”N, 05° 16’ 58.4”E). Target (◉) indicates the water quality measuring station of Charrey-sur-Saône.
Fig 2.
A) Inner and dorsal view of the Dreissena polymorpha shell. B) Infrared spectra of the shell powder.
Table 1.
Chemistry of the water and the shell of Dreissena polymorpha.
Table 2.
Contaminant concentrations in the water column, the sediments of the Saône River at the measuring station of Charrey-sur-Saône and the shell powder.
Table 3.
Accumulation factor and distribution coefficient of the most significant elements found in the shell and the water.
Fig 3.
Secondary electron images of the shell microstructure of Dreissena polymorpha.
Black boxes show location of the other views. A) Transversal section. B) Thin uppermost layer constitutes chevron-like columns. C) Crossed-lamellar layer. D) Crossed-lamellar fibres at high magnification. E) Crossed-lamellar layer based on a prismatic aggregate myostracal layer. The lower layer of the view is a complex crossed-lamellar layer. F) Innermost layer of the shell.
Table 4.
Quantification of the ASM and AIM organic matrix from Dreissena polymorpha shell.
Fig 4.
Infrared spectra of the acid soluble and the acid insoluble matrices.
a) ASM and b) AIM.
Fig 5.
Enzyme-Linked Lectin Assay (ELLA) with a set of 21 lectins against the ASM organic matrix of the Dreissena polymorpha shell.
The results were normalized to the highest response (Wheat germ agglutinin, WGA) which corresponding to 100%.
Table 5.
Monosaccharide analysis of the AIM and ASM fractions of Dreissena polymorpha shell.
Fig 6.
Capacity of different amounts of D. polymorpha ASM to inhibit the in vitro precipitation of calcium carbonate.
Different quantity of ASM are tested: ••• 10, --- 20, -•- 30 μg ASM.
Fig 7.
Influence of D. polymorpha on in vitro crystallization.
Different concentrations of D. polymorpha ASM are tested for their activity on the growth of calcium carbonate crystals. A) Blank control: no protein was added; B) 0.39 μg/mL; C) 0.78 μg/mL; D) 1.56 μg/mL; E) 3.13 μg/mL; F) 6.25 μg/mL; G) 12.5 μg/mL; H) 25 μg/mL.
Fig 8.
One-dimensional electrophoretic pattern of the ASM (lane 1) and of the LS-AIM (lane 2) on 4–20% SDS-PAGE gel with different staining.
A) Coomassie Blue stained gel (CBB). B) Alcian blue at low pH stained gel. Black points (•) highlight five discrete bands in the ASM and one in the LS-AIM (around 80 kDa). C) Silver stained gel. D) ‘Stains-all’ stained gel.
Fig 9.
Two-dimensional electrophoretic patterns of the ASM (A) and of the AIM (B).
Protein samples were loaded on a 7 cm linear pH 3–10 IPG strip and second dimension was performed with a precast 4–20% SDS-PAGE gel. ASM gel was stained with Coomassie Blue and AIM one with silver nitrate.
Table 6.
Proteins identified by searching against the Crassostrea sp., Paracentrotus lividus, FUSION homemade, NCBI ‘Other Metazoa’ and ‘Other Eukaryota’ databases.