Parvalbumin from rabbit muscle. Isolation and primary structure.
Eur. J. Biochem.1976 Nov 01;70(1):123-35. doi:10.1111/j.1432-1033.1976.tb10963.x
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摘要
A parvalbumin, with its characteristic low molecular weight (approximately 12000) acidic isoelectric point (approximately 5.5), ultraviolet spectrum (maxm 259 nm) and Ca2+-binding capacity (2 mol/mol protein) has been isolated from rabbit (Oryctolagus cuniculus) muscle. Its primary structure has been determined from a study of its tryptic peptides and of overlapping peptides generated by limited tryptic digestion and by chymotryptic and thermolytic digestions of the protein. The amino acid sequence so obtained is considered in comparison with those known for other parvalbumin and for rabbit troponin C.
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基因功能
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原始数据
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文献解读
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