Comparison of aragonitic molluscan shell proteins.
Acidic macromolecules, as a nucleation factor for mollusc shell formation, are a major focus of research. It remains unclear, however, whether acidic macromolecules are present only in calcified shell organic matrices, and which acidic macromolecules are crucial for the nucleation process by binding to chitin as structural components. To clarify these questions, we applied 2D gel electrophoresis and amino acid analysis to soluble shell organic matrices from nacre shell, non-nacre aragonitic shell and non-calcified squid shells. The 2D gel electrophoresis results showed that the acidity of soluble proteins differs even between nacre shells, and some nacre (Haliotis gigantea) showed a basic protein migration pattern. Non-calcified shells also contained some moderately acidic proteins. The results did not support the correlation between the acidity of soluble shell proteins and shell structure.
Furuhashi
Takeshi
T
Department of Molecular System Biology, University of Vienna, Althanstrasse 14, A-1090 Vienna, Austria. Takeshi_FR@hotmail.com
Miksik
Ivan
I
Smrz
Miloslav
M
Germann
Bettina
B
Nebija
Dashnor
D
Lachmann
Bodo
B
Noe
Christian
C
D000596:Amino Acids; D000818:Animals; D002113:Calcification, Physiologic; D002119:Calcium Carbonate; D015180:Electrophoresis, Gel, Two-Dimensional; D006863:Hydrogen-Ion Concentration; D008974:Mollusca / Q000033:anatomy & histology* / Q000737:chemistry* / Q000145:classification; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D012995:Solubility
D000596:Amino Acids; D011506:Proteins; D002119:Calcium Carbonate