Smith B J, Bailey J M
Nucleic Acids Res. 1979 Dec 11;7(7):2055-72. doi: 10.1093/nar/7.7.2055.
The binding of a basic 12,000 dalton protein (p12) from avian myeloblastosis virus to viral RNA and heterologous DNA has been investigated. The binding stoichiometries and constants were determined by an extrinsic fluorescence assay. In both cases each bound p12 molecule occupies four nucleotides and the apparent binding constant is approximately 1 x 10(6) M-1. Binding is non-cooperative and there is no apparent difference in the interaction of p12 with viral RNA or heterologous single-strand DNA. The relative binding constant at various ionic strengths was assayed by the nitrocellulose filter procedure. Analysis of the data revealed that each bound p12 molecule forms three ion pairs with the nucleic acid.
对来自禽成髓细胞瘤病毒的一种12,000道尔顿的碱性蛋白（p12）与病毒RNA和异源DNA的结合进行了研究。结合化学计量和常数通过外在荧光测定法确定。在这两种情况下，每个结合的p12分子占据四个核苷酸，表观结合常数约为1×10⁶ M⁻¹。结合是非协同性的，并且p12与病毒RNA或异源单链DNA的相互作用没有明显差异。通过硝酸纤维素滤膜法测定了不同离子强度下的相对结合常数。对数据的分析表明，每个结合的p12分子与核酸形成三个离子对。
