Isolation and characterization of new cross-linking amino acid "allodesmosine" from hydrolysate of elastin.
A new pentafunctional cross-linking amino acid, termed allodesmosine, was isolated from bovine ligamentum nuchae elastin. This compound was a very hygroscopic, white amorphous solid with a faint yellow tinge, soluble in aqueous solvents but not dry methanol; it was characterized by UV, FAB mass and NMR spectroscopy. The compound was shown by UV and 1H-NMR to have a pyridinium ring structure similar to desmosine. Mass spectral analysis indicated a parent compound with a mass of 655. We postulated that it arose by condensation of a reduced aldol condensation product of allysine, allysine and lysine.
Suyama
K
K
Molecular Technology of Animal Products, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Nakamura
F
F
D000596:Amino Acids / Q000302:isolation & purification*; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003432:Cross-Linking Reagents / Q000302:isolation & purification*; D003895:Desmosine / Q000302:isolation & purification*; D004549:Elastin / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry
D000596:Amino Acids; D003432:Cross-Linking Reagents; D003895:Desmosine; D004549:Elastin