Isolation and characterization of a pentameric amino acid from elastin.
An unknown amino acid was purified from bovine ligament elastin. The compound was shown by proton NMR to have a pyridinium ring structure similar to isodesmosine, yet containing an olefinic double bond on one additional side chain which was not attached to the pyridinium ring. Mass spectral analysis confirmed the NMR data and indicated a parent compound with a mass of 653. A structure is proposed that is derived from the condensation of five lysine residues. The trivial name of pentasine is proposed for this compound.
D000596:Amino Acids / Q000302:isolation & purification*; D000818:Animals; D002417:Cattle; D004549:Elastin / Q000032:analysis*; D007524:Isodesmosine / Q000031:analogs & derivatives; D008022:Ligaments / Q000032:analysis; D008239:Lysine / Q000031:analogs & derivatives; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry
D000596:Amino Acids; C052219:pentasine; D004549:Elastin; D007524:Isodesmosine; D008239:Lysine