Abstract
A new polyfunctional cross-linking amino acid was isolated from the hydrolysate of bovine ligamentum nuchae elastin. This compound was a very hygroscopic, white amorphous solid with a faint yellow tinge, and was soluble in aqueous solvents but not in dry methanol. Its proposed structure was verified by ultraviolet spectroscopy, fast atom bombardment mass spectroscopy, and 1H- and 13C-nuclear magnetic resonace spectroscopy. The data indicated it to be a pentafunctional amino acid with a quaternary pyridinium structure similar to desmosine. The mass spectral analysis indicated a parent compound with a mass of 655 (C30H51N6O10). The proposed structure is one derived from the condensation of one lysine residue and four allysine residues. Based on the names of other cross-linking amino acids found in elastin, the trivial name of allodesmosine is given for this compound. Allodesmosine was also detected in hydrolysates of bovine lung, aorta and skin by high-performance liquid chromatography.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
