Soluble proteins of the nacre of the giant oyster Pinctada maxima and of the abalone Haliotis tuberculata: extraction and partial analysis of nacre proteins
L. Bedouet et al., Soluble proteins of the nacre of the giant oyster Pinctada maxima and of the abalone Haliotis tuberculata: extraction and partial analysis of nacre proteins, COMP BIOC B, 128(3), 2001, pp. 389-400
Citations number
42
Categorie Soggetti
Biochemistry & Biophysics
Journal title
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
Several proteins from nacre of the oyster Pinctada maxima and the abalone H
aliotis tuberculata were extracted and partly characterized. Proteins dispe
rsed in aragonite were solubilized during demineralization with acetic acid
whereas proteins adsorbed on conchiolin were extracted with sodium dodecyl
sulfate and beta -mercaptoethanol. The matrix of Pinctada maxima nacre is
composed of one main protein with an apparent molecular weight of 20 kDa (p
20). This protein was found in the acetic acid soluble fraction of nacre, a
s well as in the Laemmli-solubilized extract of conchiolin. In addition, th
e p20 solubilized with acetic acid can form oligomers made of 6 monomers li
nked together by disulfide bridges. The first N-terminal 21 amino acids of
p20 were determined and no homology with known proteins was found. In Halio
tis tuberculata nacre, 5 main proteins were solubilized during demineraliza
tion and 3 glycoproteins were detected. Stains-all and Alcian blue staining
revealed polyanionic proteins in the extracts isolated from Pinctada maxim
a and Haliotis tuberculata nacre. (C) 2001 Elsevier Science Inc. All rights
reserved.