Tryptic digestion of immunoglobulin M in urea: conformational lability of the middle part of the IgM molecule.
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Biomedical subjects
Publications and source records attributed to F W Putnam.
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The amino acid sequence of the micro, chain of a human IgM immunoglobulin, including the location of all disulfide bridges and oligosaccharides, has been determined. The homology of the constant regions of immunoglobulin micro, gamma, alpha, and epsilon heavy chains reveals evolutionary relationships and suggests that two genes code for each heavy chain.
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Sequence analysis of an 1gM immunoglobulin shows that the variable regions of hunman micro and gamma1 heavy chainis may have twice as much homology as their constant regions and that evolutionary divergence of micro and gamma1 heavy chain genes occurred not long after the separation of heavy and light chain genes.
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The amino acid sequence around the central disulfide bridge linking the mu heavy chains of the human immunoglobulin M monomer is unlike that in immunoglobulin G. This hinge area contains one of the five oligosaccharides of the mu chain, is low in proline, and is the site of tryptic cleavage to yield Fabmicro and Fcmicro fragments.
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The variable regions of the light and heavy chains on the same macroglobulin (immunoglobulin M) molecule are no more related in amino acid sequence than are the variable regions of the light and heavy chains of different immunoglobulin molecules. Subgroups of micro chains are similar in their variable sequence to subgroups of gamma chains.
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