Bisphenol derivative of allysine for high-performance liquid chromatographic analysis of allysine residue of proteins.
Allysine is the most important precursor of physiologically essential cross-links formation in collagen and elastin and is formed by enzymatic oxidative deamination of lysine residues. Because it is a highly reactive aldehyde, many cross-linking amino acid residues may arise from its reaction with other allysine residues or lysine or even histidine residues. We purified and isolated an allysine bisphenol derivative, 1-amino-1-carboxy-5,5-bis-p-hydroxyphenylpentane (ACPP), from the reaction products of phenol and allysine residue of bovine ligamentum nuchae by acid hydrolysis in 6 M HCl. The structure of ACPP was verified by UV, fast atom bombardment-MS, 1H- and 13C-nuclear magnetic resonance spectroscopies. The optimal reaction condition for ACPP synthesis accompanied by hydrolysis of such proteins was investigated and an ion-paired high-performance liquid chromatographic method for determination of allysine as ACPP was also developed.
Jahanmard
E
E
Department of Bioorganic Chemistry, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Suyama
K
K
D015074:2-Aminoadipic Acid / Q000031:analogs & derivatives* / Q000032:analysis / Q000737:chemistry; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D010636:Phenols / Q000737:chemistry*; D015203:Reproducibility of Results; D013056:Spectrophotometry, Ultraviolet
D010636:Phenols; D015074:2-Aminoadipic Acid; C000061:allysine