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

作　　者：李如亮[1] 曹新文[1] 

机构地区：[1]武汉大学生物学系

出　　处：《武汉大学学报（自然科学版）》1992年第4期110-114,共5页Journal of Wuhan University(Natural Science Edition)

摘　　要：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.

关 键 词：纯化 鲫 白蛋白 肌肉 

分 类 号：Q512.1[生物学—生物化学]