[Quaternary structure of oligomeric immunoglobulin A forms from human blood serum].
A character of forces stabilyzing quaternary structure of dimer and more high molecular human immunoglobulin A oligomers is found to be different. Quaternary structure of IgA dimer is formed when joining subunits with disulfide bonds and is stabilized by non-covalent interactions between them. Disulfide bonds play a main part in the formation of trimers and tetramers. Dimer IgA reconstructs by 40% from subunits with intact interchain S--S bonds. The addition of exogenous J-chain does not significantly affect the process of dimer self-assembling from subunits with recovered and intact interchain disulfide bonds.
D055598:Chemical Phenomena; D002621:Chemistry; D004220:Disulfides; D004355:Drug Stability; D006801:Humans; D007070:Immunoglobulin A; D007144:Immunoglobulin J-Chains; D046911:Macromolecular Substances
D004220:Disulfides; D007070:Immunoglobulin A; D007144:Immunoglobulin J-Chains; D046911:Macromolecular Substances
Izuchenie chetvertichnoĭ struktury oligomernykh form immunoglobulina a iz syvorotki krovi cheloveka