Zechel K
Hoppe Seylers Z Physiol Chem. 1979 Jun;360(6):777-82. doi: 10.1515/bchm2.1979.360.1.777.
Partial tryptic cleavage products of pure actin from rabbit skeletal muscle and chicken gizzard are compared by two-dimensional electrophoresis in polyacrylamide gels with respect to isoelectric point and molecular weight. While the intact polypeptides (Mr 42,000) have different isoelectric points, two large cleavage products (Mr 35,000) generated from both both actin species have identical isoelectric points and identical molecular weights. These relatively trypsin-resistant cleavage products are presumably identical to the known "core actin" fragments which lack the aminoterminal region of the polypeptide chain. Therefore the differences that are responsible for the different isoelectric points of rabbit skeletal muscle actin and chicken gizzard actin seem to be restricted to the aminoterminal part of the actin polypeptide chains as was proposed on the basis of partial amino acid sequence data.
通过聚丙烯酰胺凝胶二维电泳，比较了兔骨骼肌和鸡砂囊纯肌动蛋白的部分胰蛋白酶裂解产物的等电点和分子量。完整的多肽（Mr 42,000）具有不同的等电点，而两种肌动蛋白产生的两个大的裂解产物（Mr 35,000）具有相同的等电点和相同的分子量。这些相对抗胰蛋白酶的裂解产物可能与已知的“核心肌动蛋白”片段相同，后者缺乏多肽链的氨基末端区域。因此，兔骨骼肌肌动蛋白和鸡砂囊肌动蛋白等电点不同的原因似乎仅限于肌动蛋白多肽链的氨基末端部分，这是根据部分氨基酸序列数据提出的。
