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. Author manuscript; available in PMC: 2010 Feb 1.
Published in final edited form as: Comp Biochem Physiol B Biochem Mol Biol. 2008 Oct 15;152(2):110–117. doi: 10.1016/j.cbpb.2008.10.004

Figure 1.

Figure 1

The effect of disrupting hydrophobic interactions, disrupting electrostatic interactions, and removing divalent ions on the solubility of glue from the slug A. subfuscus. A+ B) Quantitative analysis of the effect of the non-ionic detergent Tween-20 (0.5%) and high salt concentration (1 M NaCl) respectively. The bars in A and B show the staining intensity of bands on SDS-PAGE for the four most common proteins in the glue. Band intensities are expressed as a percentage of the total staining intensity of all four bands in the control. Several proteins of greater than 100 kDa are pooled together. The results for each show the mean ± S.D. of three trials dissolved using the same procedure. C) SDS-PAGE showing the effect of divalent ion chelation (10 mM EDTA). The position of three major bands at 15, 40 and 100 kDa is shown on the left.