Two heavy chains of 21S dynein from sea urchin sperm flagella.
Two heavy chains of 21S dynein from sea urchin sperm flagella.
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来自海胆精子鞭毛的两条 21S 动力蛋白重链。
DOI：
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发表时间：
1985
期刊：
影响因子：
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通讯作者：
Y. Yano
中科院分区：
文献类型：
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作者：
Y. Yano
研究了海胆精子鞭毛来源的21S动力蛋白及其经低盐处理解离的成分的生化特性。 SDS-尿素凝胶电泳和二维凝胶电泳表明21S动力蛋白制剂含有两条不同的重链。这两条重链，称为 A α 和 A β，显然具有相同的分子量 500,000，但在 SDS-尿素凝胶上显示出不同的迁移率。在尿素存在下，Aα和Aβ重链的等电点分别为5.7和5.2。这两条重链的蛋白水解消化模式明显不同，但氨基酸组成相似。低盐处理和蔗糖密度梯度离心可以将21S动力蛋白的组分部分分离成两部分：沉降系数较大的部分包含Aα重链，而沉降系数较小的另一部分包含Aβ重链和三个中间链。这两个部分表现出明显不同的动力学特性，因此可能在动力蛋白-微管相互作用中发挥不同的作用。
The biochemical properties of 21S dynein derived from sea urchin sperm flagella and of its components dissociated by low salt treatment were studied. SDS-urea gel electrophoresis and two-dimensional gel electrophoresis showed that the 21S dynein preparation contains two distinct heavy chains. These two heavy chains, termed A alpha and A beta, had apparently the same molecular weight of 500,000 but showed different mobilities on SDS-urea gels. The isoelectric points of A alpha and A beta heavy chains were 5.7 and 5.2, respectively, in the presence of urea. Proteolytic digestion patterns of these two heavy chains were clearly different, but the amino acid compositions were similar. Low salt treatment and sucrose density gradient centrifugation could partially separate the components of 21S dynein into two fractions: the one with larger sedimentation coefficient contained the A alpha heavy chain, and the other with smaller sedimentation coefficient contained the A beta heavy chain and three intermediate chains. These two fractions showed distinctly different kinetic properties, and thus may play different roles in dynein-microtubule interaction.