The primary structure of a cell-binding bone sialoprotein.
The primary structure of a cell-binding bone sialoprotein.
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发表时间：
1988-12
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通讯作者：
Åke Oldberg;A. Franzén;D. Heinegård
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作者：
Åke Oldberg;A. Franzén;D. Heinegård
测定了大鼠骨唾液蛋白（BSP）的氨基酸序列。该序列从一个1974碱基对cDNA中推导出一个包含320个残基的蛋白质，其中包括一个16个残基的长信号肽。成熟的BSP分子质量为33,600，主要含有谷氨酸和甘氨酸残基，占所有残基的32%。谷氨酸残基通常分布在多达10个连续残基的簇中。BSP mRNA的组织分布表明该蛋白可能是骨组织中细胞的独特产物。BSP含有Arg-Gly-Asp序列，这可能是其细胞结合特性的原因(Oldberg， A., franz<s:1>， A., heineg<s:2>， D., Pierschbacher， M.，和Ruoslahti， E.（1988）。化学。263,19433-19436)。
We have determined the amino acid sequence of rat bone sialoprotein (BSP). The sequence deduced from a 1974-base pair cDNA encodes a protein of 320 residues, including a 16-residues long signal peptide. The mature BSP has a molecular mass of 33,600 and contains predominantly glutamic acid and glycine residues, which constitute 32% of all residues. The glutamic acid residues are typically distributed in clusters of up to 10 consecutive residues. The tissue distribution of BSP mRNA suggests that the protein may be a unique product of cells in bone tissue. BSP contains an Arg-Gly-Asp sequence, which presumably is responsible for its cell binding properties (Oldberg, A., Franzén, A., Heinegård, D., Pierschbacher, M., and Ruoslahti, E. (1988) J. Biol. Chem. 263, 19433-19436).