Specific dimerization of the light chains of XXXX immunoglobulin.

@entity1 @entity2975 @entity1543 @entity1133
1. The light chains of @entity1 immunoglobulin were allowed to dimerize in vitro on removal of the dispersing agents @entity1543 or @entity1133 . 2. On electrophoresis in @entity2975 gel at pH8.8 the dimers yielded up to nine regularly spaced bands. This approximates to the number of electrophoretic components known to occur among the monomers. 3. Single electrophoretic components of the dimers were isolated from the gel, dissociated into monomers, and subjected as such to electrophoresis in @entity1133 -containing gels. Each gave two adjacent bands. 4. Similarly, after all the light chains as monomers had been subjected to electrophoresis in @entity1133 -containing gels, single electrophoretic components were isolated and allowed to dimerize. When examined now as dimers in the absence of @entity1133 , each component gave two adjacent bands. 5. These findings are explicable on the following basis. (a) The dimerization of the light chains is specific, at least inasmuch as it occurs between monomers of the same electrophoretic mobilities. (b) With the buffer constant, different light chains undergo different changes in net charge on being transferred from @entity1133 -containing to @entity1133 -free solution; in this way two different chains of the same initial charge can acquire a charge difference of 1. 6. Experiments with Bence-Jones proteins and other homogeneous light chains gave results substantiating the conclusions (a) and (b).
