Kinetics of Dimerization of the Variable Fragment of the Bence‐Jones Protein Au

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Abstract
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 200 C. The dimerization constant was about 1 × 105 M−1. The reaction enthalpy was positive and the process was entropy driven. The association and dissociation rate constants were 9×106 M−1 s−1 and 1.5×102 s−1 respectively. Temperature‐jump experiments exhibited the presence of two isomers of the dinier, which are present at equilibrium in a ratio of about 1: 1. Isomerization occurred wich a half‐life of about 0.1 s.