CHARACTERIZATION AND N-TERMINAL SEQUENCING OF A CALCIUM-BINDING PROTEIN FROM THE CALCAREOUS CONCRETION ORGANIC MATRIX OF THE TERRESTRIAL CRUSTACEAN ORCHESTIA-CAVIMANA
G. Luquet et al., CHARACTERIZATION AND N-TERMINAL SEQUENCING OF A CALCIUM-BINDING PROTEIN FROM THE CALCAREOUS CONCRETION ORGANIC MATRIX OF THE TERRESTRIAL CRUSTACEAN ORCHESTIA-CAVIMANA, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1293(2), 1996, pp. 272-276
We extracted proteins from the organic matrix of calcareous concretion
s, which represents the calcium storage form in a terrestrial crustace
an. Electrophoretic analyses of water-soluble organic-matrix proteinac
eous components revealed 11 polypeptides, 6 of which are probably glyc
osylated. Among the unglycosylated proteins, we characterized a 23 kDa
polypeptide, with an isoelectric point of 5.5, which is able to bind
calcium. Its N-terminal sequence is rich in acidic amino acids (essent
ially aspartic acid). All these characteristics suggest its involvemen
t in the calcium precipitation process within the successive layers of
the organic matrix.