Effects of potassium chloride and temperature on the kinetics of recombination of heavy and light chains of a human IgGl myeloma protein.
The effects of KCl and temperature on the kinetics of the recombination reaction of alkylated H and L chains of a human myeloma protein were studied by means of circular dichroism (CD). The recombination rate was considerably reduced by the presence of KCl. The results of the difference spectra showed that tryptophyl residue(s) in L chains are perturbed by KCl. No changes in the CD and absorption spectra with KCl concentration were observed for H chains and recombined H2L2. The change in the rate constant with KCl concentration paralleled the changes in the CD at 235 nm and the difference in molar extinction coefficient at 293 nm. These facts suggest that the reduction of the recombination rate in the presence of KCl is due to a change in the conformation of L chains as a result of specific interaction with chloride ions or by a shift to the dimer form in the monomer-dimer equilibrium of L chains. The rate constant showed a temperature dependence with an activation energy of 17.4 kcal/mole.
D001665:Binding Sites; D002942:Circular Dichroism; D006801:Humans; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D009194:Myeloma Proteins; D011189:Potassium Chloride; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature
D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D046911:Macromolecular Substances; D009194:Myeloma Proteins; D011189:Potassium Chloride