鲫鱼肌肉微白蛋白的纯化及其性质研究

鲫鱼肌肉微白蛋白的纯化及其性质研究 PURIFICATION AND PROPERTIES OF PAVALBUMIN FROM RED MUSCLE OF CARASSIUS VULGARIS 李如亮 Li Ruliang Cao Xinwen 1 first-author 曹新文 1 武汉大学生物学系 武汉大学生物学系 Department of Boilogy,Wuhan University Department of Boilogy,Wuhan University 本文建立了一个简易的方法,纯化了鲫鱼肌肉中的两种微白蛋白（Parvalbumin）。经PAGE、SDS-PAGE 和等电聚焦-PAGE 均证明为单一谱带。紫外吸收光谱分析表明为典型的苯丙氨酸特征吸收光谱。微白蛋白Ⅰ的分子量为11500,等电点为d.2.微白蛋白Ⅱ的分子量为10500,等电点为3.8.经 DNS-Cl 末端分析法证明其 N-末端是封闭的。氨基酸组成分析表明微白蛋白Ⅰ不含脯氨酸、甲硫氨酸和酪氨酸。酸性氨基酸与苯丙氮酸含量较高。园二色性光谱分析表明微白蛋白Ⅰ呈典型的α-螺旋结构,是一个典型的α-蛋白。 Two soluble calcium-binding proteins,parvalbumin（PV）,have been isolated from the red skele- tal muscle of Carassius Vulgaris.The purification procedure involved ammonium sulfate precipitation, gel filtration on Sephadex G-75 and DEAE-C.This procedure resulted in the isolation of two proteins which were homogeneous upon polyacrylamide gel electrophoresis,SDS-PAGE and isoelectric focusing PAGE.The calcium-binding proteins were found to be typical parvalbumin by the following creteri- ons:（1）Molecular weight.11500 of PV1 and 10500 of PV2.（2）pI:4.2 of PV1 and 3.8 of PV2. （3）The typical absorption spectrum of ε max at 259 nm.（4）Amino acid composition including eleven residues of phenylalanine,no tyrosine,tryptophan and proline.（5）A blocked N-terminus.These properties are the basis of the important roles of parvalbumin in metabolism and regularization. 鲫鱼 微白蛋白 纯化 Carassius Vulgaris parvalbumin purification Q959.468;Q51 1992-04-01 2021-04-01 4