The noncovalent recombination of normal human immunoglobulin light chains and their halves with normal heavy chains and of a monoclonal light chain and its constant and variable halves with the autologous heavy chain has been studied. When the recombination mixtures were analyzed at an ionic strength close to the physiologic, intact light chains recombined readily with heavy chains, whereas light chain halves showed no tendency to recombine under these conditions. At higher ionic strength some binding of constant and variable fragments to heavy chains was observed. The results indicate that in an immunoglobulin molecule both the constant and the variable half of the light chain participate in the noncovalent bonding to heavy chain and demonstrate that a covalent bond between the halves is of great importance for recombination.

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