Kinetics of dimerization of the variable fragment of the Bence-Jones protein Au.

Kinetics of dimerization of the variable fragment of the Bence-Jones protein Au.
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Bence-Jones 蛋白 Au 可变片段二聚化动力学。

DOI:
10.1111/j.1432-1033.1976.tb10866.x
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发表时间:
1976
期刊:
European journal of biochemistry
影响因子:
--
通讯作者:
Hans J. Schramm
Hans J. Schramm
中科院分区:
--
文献类型:
--
作者:
Hiroshi Maeda;Juergen Engel;Hans J. Schramm

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The dimerization of the variable fragment of the Bence-Jones protein Au was examined in phosphate buffers at pH 6.8-6.9 And ionic strength of 0.1 M or 0.2 M at 20 degrees C. The dimerization constant was about 1 X 10(5) M-1. The reaction enthalpy was positive and the process was entropy driven. The association and dissociation rate constants were 9 X 10(6) M-1 s-1 and 1.5 X 10(2) s-1 respectively. Temperature-jump experiments exhibited the presence of two isomers of the dimer, which are present at equilibrium in a ratio of about 1:1. Isomerization occurred with a half-life of about 0.1 s.