Characterization of a matrix protein in the gastroliths of the crayfish Procambarus clarkii

Bioscience, Biotechnology, and Biochemistry
K IshiiH Nagasawa

Abstract

As a first step in understanding the calcification mechanism, a matrix protein in the gastrolith of the crayfish Procambarus clarkii was purified and sequenced. The protein was insoluble in acid, but after trypsin digestion, it dissolved in 6 M urea. The trypsin-digested protein dissolved in urea solution was purified by reversed-phase HPLC and designated gastrolith matrix protein fragment. The fragment had a molecular weight of 9658 and a blocked amino terminus. It had tandemly repeated units not reported before at the central part of the sequence, with each unit being Gly-Ser-X1-X2-Phe as the most typical sequence. This peptide was found associated with chitin, a main component of the organic matrix.

Citations

Oct 8, 2013·Bioscience, Biotechnology, and Biochemistry·Hiromichi Nagasawa
May 16, 2008·Proceedings of the National Academy of Sciences of the United States of America·Assaf ShechterAmir Sagi
Feb 13, 2010·The Journal of Biological Chemistry·Lilah GlazerAmir Sagi
Aug 30, 2011·Proceedings of the National Academy of Sciences of the United States of America·Anat Akiva-TalAsher Schmidt
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Jun 7, 2000·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·T WatanabeM Kono

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