Human subjects were given 4-mg intravenous doses of a-~-aspartylglycine-l-C~~, P-Laspartylglycine-1-C 4, or an equivalent molar amount of free g1y~ine-l-C'~ and unlabeled aspartic acid. Much more radioactivity appeared in the expired carbon dioxide, in the urinary hippuric acid, and in the glycine and serine of plasma protein when the a rather than the p peptide was given. The results with free glycine and the a peptide were similar. When the p peptide was administered most of the radioactivity promptly appeared in the urine in the same chemical form but mixed with a larger quantity of endogenous p-aspartylglycine.The accompanying report from this laboratory (Buchanan et d., 1962) describes the isolation and identification of a number of B-aspartyl and yglutamyl oligopeptides from human urine. The most abundant of these, p-aspartylglycine, was shown not to arise by isomerization of a-aspartylglycine (John and Young, 1954;Swallow and Abraham, 1958; Byrant et al., 1959) during the isolation procedure, and it is likely that the other @-aspartyl oligopeptides found are actually excreted in the fl form. The present paper reports *Supported in part by Grant A-1277 from the United States Public Health Service. Preliminary reports (Haley et al., 1961; Buchanan at al., 1961) have appeared. studies on the metabolic fates of synthetic aand 8-aspartylglycines given intravenously to human subjects. The results support a hypothesis (Buchanan et aZ., 1962) that may explain the presence of P-aspartyl peptides in urine. METHODSThe wand P-L-aspartylglycines were prepared from carbobenzoxy-L-aspartic acid and glycine-l-C14 by a slight modification of the procedure of LeQuesne and Young (1952), separated chromatographically, and recrystallized from alcohol !Buchanan et d., 1962). The specific radioactivity of crystalline peptides was 2.5 pc per mg.
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