Azuma T, Isobe R, Hamaguchi K
J Biochem. 1975 Mar;77(3):473-9. doi: 10.1093/oxfordjournals.jbchem.a130748.
The recombination of alkylated H and L chains of a human myeloma protein (Jo) was studied by means of circular dichroism (CD). Marked CD changes were observed at 295 and 235 nm when H and L chains recombined. The change in the CD maximum at 235 nm was followed with time after mixing preparations of H and L chains in the pH range between 4 and 6. The recombination reaction was slow and followed second order kinetics. The observed rate constants were markedly dependent on pH. The pH dependence of the rate constant was analyzed assuming that there are two forms of H chain which are in a pH-dependent equilibrium with each other.
通过圆二色性(CD)研究了人骨髓瘤蛋白(Jo)烷基化重链和轻链的重组。当重链和轻链重组时,在295和235nm处观察到明显的CD变化。在pH值为4至6的范围内混合重链和轻链制剂后,随时间跟踪235nm处CD最大值的变化。重组反应缓慢,遵循二级动力学。观察到的速率常数明显依赖于pH值。假设存在两种相互处于pH依赖平衡的重链形式,分析了速率常数对pH的依赖性。