Characterization of a Matrix Protein in the Gastroliths of the Crayfish Procambarus clarkii
スポンサーリンク
概要
- 論文の詳細を見る
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 6M 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.
- 社団法人日本農芸化学会の論文
- 1996-09-23
著者
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Nagasawa Hiromichi
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The U
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Ishii K
Hokkaido Univ. Hokkaido Jpn
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Yanagisawa T
Utsunomiya Univ. Tochigi Jpn
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Nagasawa Hiromichi
Graduate School Of Agricultural And Life Sciences University Of Tokyo
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Nagasawa Hiromichi
Department Of Applied Biological Chemistry Graduate School Of Agriculture And Life Sciences Universi
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Nagasawa Hiromichi
Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo
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Ishii K
Transformation Laboratory Department Of Molecular And Cell Biology Forestry And Forest Products Rese
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ISHII Katsuaki
Ocean Research Institute, University of Tokyo
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YANAGISAWA Tadashi
Ocean Research Institute, The University of Tokyo
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