Brodner O G, Wieland T
Hoppe Seylers Z Physiol Chem. 1976 Jan;357(1):89-93. doi: 10.1515/bchm2.1976.357.1.89.
During the isolation of the amatoxin RNA-polymerase B-complex from calf thymus tissue we also isolated a protein (ABP) which shows such strong affinity to [3H)amanin that significant binding occurs at low concentrations (10-7M) of the label. The presence of a new amatoxin-complex is demonstrated by coprecipitation of amatoxin and ABP with ammonium sulphate and the common chromatography on phosphocellulose and Sephadex G-25. The new protein ABP is characterized by denaturating sodium dodecylsulphate-gel electrophoresis. The molecular masses of both main bands - possibly subunits of ABP - are determined as 100000 and 10000 - 15000 Dalton and different from the subunit pattern of RNA-polymerases B and C.
从小牛胸腺组织中分离鹅膏毒肽RNA聚合酶B复合物时，我们还分离出一种蛋白质（ABP），它对[3H]鹅膏覃碱具有很强的亲和力，以至于在低浓度（10-7M）标记物时就会发生显著结合。通过硫酸铵共沉淀鹅膏毒肽和ABP以及在磷酸纤维素和葡聚糖G-25上的共同层析，证明了一种新的鹅膏毒肽复合物的存在。新蛋白质ABP通过十二烷基硫酸钠变性凝胶电泳进行表征。两条主要条带（可能是ABP的亚基）的分子量测定为100000和10000 - 15000道尔顿，与RNA聚合酶B和C的亚基模式不同。
