Abstract
Urinary peptides were roughly fractionated by combined columns of cation and anion exchange resins, and the peptides eluted from each column were further fractionated by a combination of various ion exchange resins and DEAF-cellulose column chromatography, paper chromatography and other methods. From the fractions adsorbed on cation exchange resin, 13 homogeneous peptides could be isolated, and from the ones adsorbed on anion exchange resin, 8 glycopeptides could be found. Their amino acid compositions were analyzed. Although some fractions remain univestigated, an outline of the whole aspect of main urinary peptides has been clarified by this study.
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