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- W2078051925 abstract "Irradiation of lyophilized ovalbumin with y-rays causes the formation of a wide spectrum of protein molecules in various stages of structural degradation (1). In addition, solutions of the irradiated ovalbumin contain more nonprotein nitrogen than solutions of native protein (2). As part of a series of studies on the nature of radiation-induced fragments, solutions of y-irradiated ovalbumin were studied by means of one-dimensional paper chromatography using four solvent systems: Phenol: water, n-butanol: acetic acid: water, borate buffer: m-cresol: phenol, and lutidine: collidine: diethylamine: water." @default.
- W2078051925 created "2016-06-24" @default.
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- W2078051925 date "1963-01-01" @default.
- W2078051925 modified "2023-09-25" @default.
- W2078051925 title "Paper-Chromatographic Separations of Fragments from g-Irradiated Ovalbumin" @default.
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- W2078051925 doi "https://doi.org/10.2307/3626553" @default.
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