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• W1993896155 abstract "When α 2 ‐macroglobulin ( α 2 M) from the American horseshoe crab, Limulus polyphemus , reacts with proteinases, its thiol esters, like those of other α‐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 α‐macroglobulins extensively form crosslinks to the reacting proteinase, Limulus α 2 M does not. It rather becomes internally crosslinked. It was found from N‐terminal sequence analysis of purified [ 14 C]carboxymethylated peptides from Limulus α 2 M‐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." @default.
• W1993896155 created "2016-06-24" @default.
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• W1993896155 date "1996-09-09" @default.
• W1993896155 modified "2023-10-14" @default.
• W1993896155 title "Localisation of the major reactive lysine residue involved in the selfcrosslinking of proteinase-activated<i>Limulus</i><i>α</i>₂-macroglobulin" @default.
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• W1993896155 doi "https://doi.org/10.1016/0014-5793(96)00852-6" @default.
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