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- W2013826503 abstract "1.|Homocysteine thiolactone (HTL) is proposed as a reagent for introducing thiol groups into proteins. HTL is analogous to N-acetylhomocysteine thiolactone (AHTL), except that the unblocked amino group permits a polymeric accumulation of homocysteinyl residues; hence several thiol groups may be introduced for each protein group attacked. 2.|Relevant differences in properties between HTL and AHTL were established in the absence of protein. 3.|Thiolation of immunoglobulin G (IgG) was best performed with imidazole catalysis at pH 9.6–10, in the presence of methylmercuric hydroxide to block and label the thiol groups. At a lower pH, mutual interaction of HTL molecules and precipitation of by-products promoted irreversible denaturation of the protein. A high concentration of all reactants and a large excess of HTL relative to protein favoured a high mercury content in the final product. 4.|A single treatment of IgG with HTL and mercurial could effect binding of mercury equivalent to 11% of the weight of the protein, or more, but further labelling was possible. The methylmercury label was stable to gel filtration and to concentration of the protein by ultrafiltration, and there had been no degradation to inorganic mercury. 5.|The nature of the labelled product is discussed, and parallels and distinctions are drawn between treatment of proteins with HTL and the introduction of polypeptidyl residues with N-carboxyamino acid anhydrides." @default.
- W2013826503 created "2016-06-24" @default.
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- W2013826503 date "1972-01-01" @default.
- W2013826503 modified "2023-10-15" @default.
- W2013826503 title "Thiolation of proteins with homocysteine thiolactone: Preparation of immunoglobulin g heavily labelled with methylmercury" @default.
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- W2013826503 doi "https://doi.org/10.1016/0005-2795(72)90258-9" @default.
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