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本文用Sephadex G-50凝胶过滤和DEAE-52离子交换柱层析提纯了电鳗(Electrophorus electricus)肌肉中的两种微白蛋白(parvalbumin)。350g新鲜肌肉可提取100—150mg纯的微白蛋白Ⅰ,等电点为4.25。微白蛋白Ⅱ的含量约为组份Ⅰ的1/5,它的等电点为3.85。根据胰蛋白酶水解所得肽段和溴化氰裂解片段的氨基酸序列,以及微白蛋白一级结构的同源性确定了两种微白蛋白的氨基酸全序列。微白蛋白Ⅰ和微白蛋白Ⅱ的序列有22个氨基酸残基差异,但和Ca~(++)离子结合有关的氨基酸残基并无变异。
In this paper, two kinds of parvalbumins in muscle of Electrophorus electricus were purified by Sephadex G-50 gel filtration and DEAE-52 ion exchange column chromatography. 350g of fresh muscle extract 100-150mg of pure microalbumin I, pI 4.25. The content of microalbumin II is about 1/5 of that of component I, and its isoelectric point is 3.85. Based on the amino acid sequences of tryptic peptides and cyanogen bromide cleaved fragments and the homology of the primary structure of microalbumin, the complete amino acid sequences of the two microalbumin proteins were determined. There were 22 amino acid residues in the sequence of microalbumin I and microalbumin II, but there was no mutation in the amino acid residues related to Ca ~ (++) ion binding.