The basic features of "y-globulin synthesis and assembly have been elucidated in hyperimmune rabbit lymph nodes and malignant tissues of the mouse (1-12). These studies indicate that heavy (H) and light (L) chains are synthesized independently on ribosomes of different sizes (3, 4) and that L chains are then released from their ribosomes into an intracellular pool (5). No equivalent pool of soluble (released) intracellular H chains has been demonstrated (6). In at least four mouse tumors, L chains combine with nascent H chains on polyribosomes before their release (3, 6, 7). The assembly of "y-globulin occurs intracellularly (8, 9), and there is a 20 to 30 minute lag between the synthesis of chains and their secretion (9). During this period, the attachment of the major part of the carbohydrate moieties takes place (11).The relative amounts of H and L chains synthesized and the patterns of assembly differ in several of the immunoglobulin synthesizing tissues studied to date. Some malignant and hyperimmune cells appear to be balanced with respect to the number of L and H chains secreted while others secrete excess free light chains. There is also evidence that the H-L dimer serves as an intermediate in the assembly of "y-globulin by some mouse plasmacytomas while others are assembled primarily through an H-H dinaer (6, 9, 12). G a m m a globulin synthesis by malignant tissues from humans with multiple myeloma has been examined (13, 14) but a systematic study of this process in various types of human plasma cell tumors has not yet been performed. The