Chromatographic study of the interrelationships of immunoglobulin A and alpha 1-microglobulin in myelomatosis.
The binding of alpha 1-microglobulin (alpha 1-m) to serum immunoglobulin A (IgA) myeloma proteins have been examined by analytical and preparative Superose high-performance gel chromatography. Enzyme immunoassays showed that in the serum alpha 1-m was bound to monomeric IgA, but not to the polymeric IgA, and was also present in a free form. The IgA-alpha 1-m complexes involved covalent and non-covalent bonds. Considerable variation in the ratio of bound to unbound forms of alpha 1-m was observed that appears to be a result of variation of the IgA alpha heavy chains. Reduction of monomeric IgA produced alpha 1-m-heavy chain complexes, free alpha 1-m, light and alpha heavy chains, and traces of alpha 1-m attached to IgA that was resistant to reduction.
Cooper
E H
EH
Johns
E A
EA
Itoh
Y
Y
Webb
J R
JR
D000510:Alpha-Globulins / Q000032:analysis*; D000818:Animals; D002021:Buffers; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006041:Goats / Q000276:immunology; D006801:Humans; D007120:Immunochemistry; D007122:Immunoelectrophoresis; D007070:Immunoglobulin A / Q000032:analysis*; D007163:Immunosorbent Techniques; D009101:Multiple Myeloma / Q000276:immunology*
D000510:Alpha-Globulins; D002021:Buffers; D007070:Immunoglobulin A; C016001:alpha-1-microglobulin