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- W2019192603 abstract "p-Hydroxyphenylglyoxal reacts with arginine residues in proteins to give a single product which can be quantitated spectrophotometrically. The reaction takes place under mild conditions, pH 7–9 and 25°C. Under these conditions up to complete modification of Nα-citraconyl-l-arginine was obtained within 60 min with less than 5% modification of other common amino acid side chains. The extent of modification in a protein can be determined at 340 nm using the molar absorption coefficient of 1.83 × 104m−1 cm−1 for the product at pH 9.0 and 25°C following removal of excess reagent by gel filtration. Several proteins, previously shown to have essential arginines, were modified by p-hydroxyphenylglyoxal and the losses in arginines were determined spectrophotometrically. These results were in close agreement with those of previous investigators. Rhea ovomucoid, a glycoprotein without arginines but containing an essential lysine, was relatively unaffected." @default.
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- W2019192603 title "Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal" @default.
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- W2019192603 doi "https://doi.org/10.1016/0003-2697(80)90006-8" @default.
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