Abstract
Dietary gelatin significantly elevated the urinary excretion of β-aspartylglycine in humans. The peptide was also found in enzymic digests of collagen prepared by the sequential action of collagenase, Pronase, and the combination of prolidase and leucinaminopeptidase. Nonenzymic conversion of normally occurring α-aspartylglycine to the β-peptide may explain the presence of the peptide in digests of lysozyme and to some extent the high levels in collagen. However, the greater amounts found in polymerized fibrin compared with fibrinogen indicate an enzymic formation of the peptide bond during polymerization. In agreement with the theory that β-aspartylglycine bonds link polypeptide chains of certain proteins was the finding of more β-aspartylglycine in the highly cross-linked Achilles tendon collagen than in skin collagen.
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