Isolation and structural characterization of a new crosslinking amino acid, cyclopentenosine, from the acid hydrolysate of elastin.
A novel polyfunctional crosslinking amino acid, which was developed slower than lysinonorleucine and faster than desmosine on thin layer chromatography, was isolated from the hydrolysate of bovine aorta elastin. Its proposed structure was verified by ultraviolet spectroscopy, fast atom bombardment mass spectroscopy, and nuclear magnetic resonance spectroscopy. The data indicated it to be a trifunctional amino acid with a cyclopentene structure. The mass spectral analysis indicated a parent compound with a mass of 381 (C18H27N3O6). The proposed structure is one derived from the condensation of three allysine residues. Based on the names of other crosslinking amino acids found in elastin, the trivial name of cyclopentenosine is given to this compound.
Nakamura
F
F
Laboratory of Molecular Technology of Animal Products, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Yamazaki
K
K
Suyama
K
K
D000596:Amino Acids / Q000737:chemistry / Q000302:isolation & purification*; D000818:Animals; D001011:Aorta / Q000737:chemistry; D002417:Cattle; D003432:Cross-Linking Reagents / Q000302:isolation & purification; D004549:Elastin / Q000737:chemistry*; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D015394:Molecular Structure; D010875:Pipecolic Acids / Q000737:chemistry / Q000302:isolation & purification*; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D003432:Cross-Linking Reagents; D010875:Pipecolic Acids; C076144:cyclopentenosine; D004549:Elastin