STUDIES OF SELF-ASSOCIATION OF BACTERIOPHAGE-T4 GENE 32 PROTEIN BY EQUILIBRIUM SEDIMENTATION
STUDIES OF SELF-ASSOCIATION OF BACTERIOPHAGE-T4 GENE 32 PROTEIN BY EQUILIBRIUM SEDIMENTATION
复制标题
DOI：
10.1016/0022-2836(75)90380-0
复制
发表时间：
1975-01-01
影响因子：
5.6
通讯作者：
GOLDTHWAIT, DA
中科院分区：
文献类型：
--
作者：
CARROLL, RB;NEET, K;GOLDTHWAIT, DA
噬菌体T4基因32蛋白的自结合已在不同条件下在分析超速离心机中被检测，以确定该过程的性质。这个过程不是简单的与一个缔合常数(单体、二聚体、三聚体等)的不确定缔合。该过程的复杂性表现为：(1)在二聚体区域(在pH为10，在0.04M-MgCl2中，随着离子强度的增加，在19℃和寡核苷酸d(PT)10存在下，随着离子强度的增加，观察到的分子量-浓度曲线的特殊性)，(2)在甘油或寡聚[d(PT)4]存在下，缔合曲线的S型增加，以及(3)在pH值约为9.4时，四聚体缔合曲线的不连续性。具有两个独立变化的缔合常数(单体、二聚体、四聚体等)的模型。解释了许多发现。然而，需要一个更复杂的模型来解释在蛋白质浓度较高时，哪些曲线在二聚体处具有平台性，并增加关联性。因此，在所考察的所有条件下，有证据表明蛋白质-蛋白质相互作用不止一种类型。这些不同的相互作用可能涉及重组等生理功能。
The self-association of the bacteriophage T4 gene 32 protein has been examined in the analytical ultracentrifuge under varying conditions to determine the nature of the process. The process is not a simple indefinite association with one association constant (monomer dimer trimer etc.). The complexity of the process is shown by (1) peculiarities in the molecular weightversusconcentration curves, in the region of the dimer (observed with increasing ionic strength, at pH 10, in 0.04m-MgCl2, with aged preparations, at 19 °C and in the presence of the oligonucleotide d(pT)10), (2) the increased sigmoidicity of the association curve in the presence of glycerol or oligo[d(pT)4], and (3) the discontinuity in the association curve at the tetramer at a pH value of approximately 9.4. A model with two association constants which could vary independently (monomer dimer tetramer etc.) explained many of the findings. However, a more complex model was required to explain curves which had a plateau at the dimer with increased association at higher protein concentrations. Thus, under all conditions examined there is evidence for more than one type of protein-protein interaction. These different interactions may be involved in a physiological function such as recombination.