Mabuchi I
J Biochem. 1979 Dec;86(6):1785-93. doi: 10.1093/oxfordjournals.jbchem.a132700.
The 95,000 molecular weight protein (95K protein) of the false discharges of Limulus sperm, purified by means of preparative gel electrophoresis in the presence of sodium dodecyl sulfate, was compared with a 95K protein from Limulus muscle and chicken gizzard alpha-actinin. The results were as follows. 1) One-dimensional peptide mapping using four different proteases showed differences among these proteins. 2) Two-dimensional peptide mapping using trypsin showed that about 30% of the peptides in the digest of the sperm 95K protein were similar to those of chicken gizzard alpha-actinin and about 50% of the peptides were similar to those of the Limulus muscle 95K protein. 3) The sperm 95K protein contained relatively large amounts of Gly, Pro, and Ser and relatively small amounts of Glu and Leu compared to the muscle proteins. 4) Antibodies against the sperm 95K protein did not cross-react with the Limulus muscle 95K protein or chicken gizzard alpha-actinin. These results suggest that the 95K protein of sperm is different from alpha-actinin in primary structure.
通过在十二烷基硫酸钠存在下进行制备性凝胶电泳纯化的鲎精子假放电的95,000分子量蛋白质（95K蛋白质），与来自鲎肌肉和鸡肫α-肌动蛋白的95K蛋白质进行了比较。结果如下：1）使用四种不同蛋白酶的一维肽图谱显示这些蛋白质之间存在差异。2）使用胰蛋白酶的二维肽图谱显示，精子95K蛋白质消化物中约30%的肽与鸡肫α-肌动蛋白的肽相似，约50%的肽与鲎肌肉95K蛋白质的肽相似。3）与肌肉蛋白质相比，精子95K蛋白质含有相对大量的甘氨酸、脯氨酸和丝氨酸，以及相对少量的谷氨酸和亮氨酸。4）针对精子95K蛋白质的抗体不与鲎肌肉95K蛋白质或鸡肫α-肌动蛋白发生交叉反应。这些结果表明，精子的95K蛋白质在一级结构上与α-肌动蛋白不同。
