Boguslawski G, Kobayashi G S, Schlessinger D, Medoff G
J Bacteriol. 1975 May;122(2):532-7. doi: 10.1128/jb.122.2.532-537.1975.
An inhibitor of ribonucleic acid polymerases has been obtained from the mycelial phase of Histoplasma capsulatum and partially characterized. The inhibitor, called histin, was purified 200-fold by heat treatment at 100 C and electrophoresis on polyacrylamide gels. Histin moved in electrophoresis as if negatively charged; it was insensitive to treatment with ribonuclease of deoxyribonuclease but was completely digested by Pronase. Sucrose gradient centrifugation suggests a molecular weight of 24,000. The possibility of a regulatory role for histin in the life cycle of H. capsulatum is discussed.
一种核糖核酸聚合酶抑制剂已从荚膜组织胞浆菌的菌丝体阶段分离得到，并进行了部分特性鉴定。这种名为组菌素的抑制剂通过在100℃热处理及聚丙烯酰胺凝胶电泳纯化了200倍。组菌素在电泳中移动时似乎带负电荷；它对核糖核酸酶或脱氧核糖核酸酶处理不敏感，但能被链霉蛋白酶完全消化。蔗糖梯度离心表明其分子量为24,000。文中讨论了组菌素在荚膜组织胞浆菌生命周期中发挥调节作用的可能性。
