The Biologist in me is beginning to want to experiment. For all you SPS nuts, I am going to be making my own concoction here soon based on a couple studies below:
In vitro regulation of CaCO3 crystal growth by the highly acidic proteins of calcitic sclerites in soft coral, Sinularia polydactyla. Rahman, M. Azizur; Oomori, Tamotsu. Department of Chemistry, Faculty of Science, University of the Ryukyus, Okinawa, Japan. Connective Tissue Research (2009), 50(5), 285-293.
Abstract
Acidic proteins are generally thought to control mineral formation and growth in biocalcification. Anal. of proteinaceous components in the sol. and insol. matrix fractions of sclerites in Sinularia polydactyla indicates that aspartic acid composes about 60% of the insol. and 29% of the sol. matrix fractions. We previously analyzed aspartic acids in the matrix fractions (insol. = 17 mol%; sol. = 38 mol%) of sclerites from a different type of soft coral, Lobophytum crassum, which showed comparatively lower aspartic acid-rich proteins than S. polydactyla. Thus, characterization of highly acidic proteins in the org. matrix of present species is an important first step toward linking function to individual proteins in soft coral. Here, we show that aspartic-acid rich proteins can control the CaCO3 polymorph in vitro. The CaCO3 ppts. in vitro in the presence of aspartic acid-rich proteins and 50 mM Mg2+ was verified by Raman microprobe anal. The matrix proteins of sclerites demonstrated that the aspartic-acid rich domain is crucial for the calcite pptn. in soft corals. The cryst. form of CaCO3 in the presence of aspartic acid-rich proteins in vitro was identified by X-ray diffraction and, revealed calcitic polymorphisms with a strong (104) reflection. The structure of soft coral org. matrixes contg. aspartate-rich proteins and polysaccharides was assessed by Fourier transform IR spectroscopy. These results strongly suggest that the aspartic acid-rich proteins within the org. matrix of soft corals play a key role in biomineralization regulation.
Characterization of proteins from the matrix of spicules from the alcyonarian, Lobophytum crassum. Rahman, M. Azizur; Isa, Yeishin. Department of Marine and Environmental Sciences, Graduate School of Engineering and Science, University of the Ryukyus, 1 Senbaru, Nishihara-cho, OkinawaNishihara-cho, Okinawa, Japan. Journal of Experimental Marine Biology and Ecology (2005), 321(1), 71-82.
Abstract
The org. matrix of spicules of the alcyonarian coral, Lobophytum crassum, was studied to investigate its mol. characteristics and functional properties. The shape of the spicules was identified using SEM. The sol. org. matrix comprised 0.03% of the spicule wt. The SDS-PAGE anal. of the prepn. showed four protein bands with apparent mol. wts. of 37, 48, 67 and 102 kDa. The 67- and 102-kDa proteins appeared to be calcium binding proteins, detected as radioactive bands by 45Ca autoradiog. The 67-kDa protein appears to be glycosylated. The N-terminal amino acid sequence of the 67 kDa was detd.; 7 of 20 residues were acidic. A database search for homologous proteins did not give a clear indication of the function of the 67-kDa protein. The isolated org. matrix possesses carbonic anhydrase activity which functions in calcium carbonate crystal formation, indicating that org. matrix is not only structural protein but also a catalyst. An interpretation of these results is that the spicule of alcyonarian corals has a proteinaceous org. matrix related to the calcification process.