Someya A, Tanaka N
J Antibiot (Tokyo). 1979 Feb;32(2):156-60. doi: 10.7164/antibiotics.32.156.
Skeletal muscle actin was found by centrifugation, turbidity, and viscosity measurements to form polymers upon addition of aminoglycosides, viomycin, polymyxin B, and tetracycline. A linear relationship was observed between the amount of actin polymerization and the number of primary amino groups on the aminoglycoside antibiotics except kanamycin. Of the antibiotics studied, neomycin was most efficient in actin polymerization. Polymerization of actin was not significantly induced by kasugamycin, chloramphenicol, erythromycin, benzylpenicillin, angustmycin A, formycin, actinomycin D, and mitomycin C. Aminoglycosides and viomycin were demonstrated to inhibit the acto-HMM Mg(2+)-ATPase reaction but did not significantly affect HMM Mg(2+)-ATPase activity. It was found by equilibrium dialysis that [(3)H]dihydrostreptomycin bound to actin.
通过离心、浊度和粘度测量发现,在添加氨基糖苷类药物、紫霉素、多粘菌素B和四环素后,骨骼肌肌动蛋白会形成聚合物。除卡那霉素外,在氨基糖苷类抗生素上观察到肌动蛋白聚合量与伯氨基数量之间存在线性关系。在所研究的抗生素中,新霉素在肌动蛋白聚合方面最有效。春雷霉素、氯霉素、红霉素、苄青霉素、安古霉素A、间型霉素、放线菌素D和丝裂霉素C未显著诱导肌动蛋白聚合。氨基糖苷类药物和紫霉素被证明可抑制肌动蛋白 - 重酶解肌球蛋白Mg(2 +)-ATP酶反应,但对重酶解肌球蛋白Mg(2 +)-ATP酶活性没有显著影响。通过平衡透析发现[(3)H]二氢链霉素与肌动蛋白结合。