Bronstein W W, Knull H R
Can J Biochem. 1981 Jul;59(7):494-9. doi: 10.1139/o81-069.
Purified glycolytic enzymes were individually chromatographed through columns of Sepharose 4B containing a covalently bound F-actin-tropomyosin complex. Five of these enzymes, aldolase, glyceraldehyde-phosphate dehydrogenase, lactate dehydrogenase, pyruvate kinase, and phosphoglycerate kinase were able to interact with the complex. Glucosephosphate isomerase, triosephosphate isomerase, phosphoglycerate phosphomutase, and enolase did not bind to the F-actin-tropomyosin matrix. One nonbinding enzyme, phosphoglycerate phosphomutase, was observed to interact with F-actin-tropomyosin if the column was preloaded with lactate dehydrogenase. Since at least four other glycolytic enzymes did not associate with actin directly, it is suggested that if a glycolytic enzyme complex exists, these nonadsorbing enzymes must interact with one or more of the enzymes which do bind to actin.
将纯化的糖酵解酶分别通过含有共价结合的F-肌动蛋白-原肌球蛋白复合物的琼脂糖4B柱进行层析。其中五种酶，醛缩酶、磷酸甘油醛脱氢酶、乳酸脱氢酶、丙酮酸激酶和磷酸甘油酸激酶能够与该复合物相互作用。葡萄糖磷酸异构酶、磷酸丙糖异构酶、磷酸甘油酸磷酸变位酶和烯醇化酶不与F-肌动蛋白-原肌球蛋白基质结合。如果柱子预先用乳酸脱氢酶加载，观察到一种不结合的酶，磷酸甘油酸磷酸变位酶与F-肌动蛋白-原肌球蛋白相互作用。由于至少还有其他四种糖酵解酶不直接与肌动蛋白结合，因此表明如果存在糖酵解酶复合物，这些不吸附的酶必须与一种或多种与肌动蛋白结合的酶相互作用。
