Teague W M, Henney H R
Biochim Biophys Acta. 1976 May 20;434(1):118-25. doi: 10.1016/0005-2795(76)90041-6.
The malate dehydrogenase isoenzymes from Physarum polycephalum have been purified to homogeneity as confirmed by gel filtration chromatography, polyacrylamide gel disc electrophoresis and analytical ultracentrifugation. Certain physical and chemical parameters of the malate dehydrogenase isoenzymes reported here include sedimentation, molecular weight and subunit molecular weight. Most unique of the differences between the isoenzymes were the widely separate isoelectric points of 9.83 for mitochondrial malate dehydrogenase and 6.14 for the supernatant malate dehydrogenase. The amino acid analyses of each form were done revealing the isoenzymes were unquestionably unique proteins differing in the content of ten amino acids.
多头绒泡菌中的苹果酸脱氢酶同工酶已通过凝胶过滤色谱法、聚丙烯酰胺凝胶圆盘电泳法和分析超速离心法纯化至同质。本文报道的苹果酸脱氢酶同工酶的某些物理和化学参数包括沉降系数、分子量和亚基分子量。同工酶之间最显著的差异是线粒体苹果酸脱氢酶的等电点为9.83，而上清液苹果酸脱氢酶的等电点为6.14，两者相差很大。对每种形式进行的氨基酸分析表明，这些同工酶无疑是独特的蛋白质，在十种氨基酸的含量上有所不同。
