Beilstein J. Nanotechnol.2011,2, 222–227, doi:10.3762/bjnano.2.26
].
Figure 3 shows the result of the protein–crystal binding experiment. The proteins in the shell from Haliotis laevigata that were insoluble in 6% acetic acid were removed from the chitin core with an SDS/DTT/Tris buffer as described in the experimental section. This protein solution contained several
proteins or protein fragments visible in lane P on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in Figure 3. The protein solution was gel-filtered to remove the SDS and DTT. The obtained gel-filtered protein solution (lane gfP) shows the major bands on SDS-PAGE. The gel-filtered
protein solution was incubated with aragonite or calcite microcrystals. After incubation, the supernatant liquid from the aragonite or calcite microcrystals was removed and subjected to SDS-PAGE at two different concentrations (AS, AS* and CS, CS*). The crystals were washed 3 times with a NaCl/Tris