Abstract
Sera of five patients with Lactate dehydrogenase (LDH)-Immunoglobulin A (IgA) Kappa (K) complexes and two patients with LDH-Immunoglobulin G (IgG) Lambda (L) complexes were analized. IgA K separated from the LDH-IgA complexes reassociate with the LDH-2 and LDH-3 isoenzymes.
IgG L obtained from LDH-IgG complexes reassociated with the LDH-4 and LDH-5 isoenzymes to form LDH-IgG complexes. The results of our experiments suggest that IgA K has antigenic properties against the H2M trimer molecule which is common to LDH-2 and LDH-3 and that IgG L has antigenic properties against the M3 trimer common to LDH-4 and LDH-5.
