The stoichiometry of J chain in human secretory dimeric IgA.
Dimeric human secretory IgA was completely reduced with mercaptoethanol and alkylated with [14C]iodoacetamide. The component polypeptide chains were separated by high performance gel filtration in 5 M guanidine HCl into two fractions: one containing secretory component (SC) + heavy (H) chains; and the second containing light (L) + J chains. L and J chains were subsequently separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS) or in alkaline urea. Calculations of the J chain stoichiometry in the dimeric secretory IgA (S-IgA) molecule were based on: the measurement of the ratio of radioactivities of SC + H chain and L + J chain-fractions or L chain- and J chain-fractions; the known stoichiometry of SC, H and L chains; and the known number of half-cystine residues in the component polypeptide chains of S-IgA molecule. The data demonstrated that one molecule of dimeric S-IgA contains approx. one J chain.
D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007071:Immunoglobulin A, Secretory; D007144:Immunoglobulin J-Chains
D007071:Immunoglobulin A, Secretory; D007144:Immunoglobulin J-Chains