Chemistry of the water and the shell of <i>Dreissena polymorpha</i>.

<p>Chemistry of the water and the shell of <i>Dreissena polymorpha</i>.</p

The Shell of the Invasive Bivalve Species <i>Dreissena polymorpha</i>: Biochemical, Elemental and Textural Investigations - Fig 2

<p>A) Inner and dorsal view of the <i>Dreissena polymorpha</i> shell. B) Infrared spectra of the shell powder.</p

Secondary electron images of the shell microstructure of <i>Dreissena polymorpha</i>.

<p>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.</p

Capacity of different amounts of <i>D</i>. <i>polymorpha</i> ASM to inhibit the <i>in vitro</i> precipitation of calcium carbonate.

<p>Different quantity of ASM are tested: ••• 10, <b>---</b> 20, <b>-•-</b> 30 μg ASM.</p

Infrared spectra of the acid soluble and the acid insoluble matrices.

<p>a) ASM and b) AIM.</p

Quantification of the ASM and AIM organic matrix from <i>Dreissena polymorpha</i> shell.

<p>Quantification of the ASM and AIM organic matrix from <i>Dreissena polymorpha</i> shell.</p

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.

<p>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.</p

Location of the sampling site in the Saône River.

<p>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.</p

Enzyme-Linked Lectin Assay (ELLA) with a set of 21 lectins against the ASM organic matrix of the <i>Dreissena polymorpha</i> shell.

<p>The results were normalized to the highest response (Wheat germ agglutinin, WGA) which corresponding to 100%.</p

Two-dimensional electrophoretic patterns of the ASM (A) and of the AIM (B).

<p>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.</p