Abstract
THE isolation and chemical characterization of two new amino-acids, desmosine and isodesmosine, which form bridge-points between peptide chains in elastin has already been described1–3. The isomeric compounds are 1,3,4,5- and 1,2,3,5-tetra-substituted pyridinium salts with the empirical formula C24H40N5O8Cl (as the chloride). Consideration of the structure of the two compounds and their location as cross-bridges between peptide chains led Partridge et al.4 to suggest a possible biosynthetic route through ring closure on four lysine residues pre-existing in the peptide chains of a soluble pro-elastin.
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References
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PARTRIDGE, S., ELSDEN, D., THOMAS, J. et al. Incorporation of Labelled Lysine into the Desmosine Cross-bridges in Elastin. Nature 209, 399–400 (1966). https://doi.org/10.1038/209399b0
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DOI: https://doi.org/10.1038/209399b0
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