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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Localisation of the major reactive lysine residue involved in the self-crosslinking of proteinase- activated Limulus alpha 2-macroglobulin.

When alpha 2-macroglobulin (alpha 2M) from the American horseshoe crab, Limulus polyphemus, reacts with proteinases, its thiol esters, like those of other alpha-macroglobulins, become activated, leading to the formation of covalently crosslinked species that can be detected as high molecular weight bands in reducing SDS-PAGE. While other alpha-macroglobulins extensively form crosslinks to the reacting proteinase, Limulus alpha 2M does not. It rather becomes internally crosslinked. It was found from N-terminal sequence analysis of purified [14C]carboxymethylated peptides from Limulus alpha 2M-trypsin complexes that an isopeptide bond formed in approx. 60% yield from the thiol esterified Gln-1002 specifically to Lys-254 in the opposing monomer of the disulphide bridged dimer is the main cause of the internal crosslinking.[1]

References

  1. Localisation of the major reactive lysine residue involved in the self-crosslinking of proteinase-activated Limulus alpha 2-macroglobulin. Dolmer, K., Husted, L.B., Armstrong, P.B., Sottrup-Jensen, L. FEBS Lett. (1996) [Pubmed]
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