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Abstract
Nitroso-naphthol reacts with tyrosine-containing peptides, yielding intensely fluorescent condensation products, probably benzphenoxazinone derivatives. The condensation products of tyrosine and angiotensin migrate much slower on a Sephadex G 25 column than do the native compounds, the retardation probably being caused by the increased aromaticity of the condensation products. These observations make it possible to purify and measure tyrosine-containing peptides.
Published Version
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