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- W2009249105 abstract "A method is described for the routine succinylation of proteins using [14C]succinic anhydride as a means of measuring free ϵ-amino groups. Maximal succinylation was achieved using 6M guanidine hydrochloride as protein solvent and an 80-fold molar excess of succinic anhydride relative to total lysine residues. Treatment with hydroxylamine (pH 13, 25°C, 5 min) removed unwanted O-succinyl esters. Succinylated protein was precipitated with trichloroacetic acid, residual label washed out with ethanol and the extent of labelling measured in a scintillation counter. The method gave close to theoretical values (n.s., P >0.05) for lysyl residues in egg white lysozyme, bovine haemoglobin, ovalbumin and bovine serum albumin but gave a low value with β-lactoglobulin and an overestimate with insulin attributable to the relatively high contribution of α- relative to ϵ-amino groups in this low molecular weight protein. The method gave good results for 12 soya protein samples and was shown to be very sensitive to ‘isopeptide-type’ heat damage in these samples. The results correlated well (r = 0.91) with those obtained by the well established dye-bound lysine difference procedure whereas, as could be expected, both these methods correlated poorly with total lysine determinations (r=0.69 for succinic anhydride and r=0.77 for the dye-binding method). The proposed method shows promise as a rapid procedure for the estimation of available lysine, but further studies are necessary to test its ability to measure nutritionally available lysine in all categories of heat damage." @default.
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- W2009249105 title "An isotopic method for determining chemically reactive lysine based on succinylation" @default.
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- W2009249105 doi "https://doi.org/10.1002/jsfa.2740350418" @default.
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