| 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. |
