Polyclonal anti-desmosine antiserum is specific to desmosine molecule: no cross-reaction to pyridinoline.
Inhibition ELISA assay was used to examine the cross-reaction of the polyclonal anti-desmosine antiserum produced in rabbit against molecules possessing a "pyridinium ring" as their core structure i.e. isodesmosine, pentasine, pyridinoline and 2'-deoxypyridinoline, highly purified with column chromatography, and structurally unrelated substances, i.e. cysteic acid, taurine and 2-aminopyridine (core structure of desmosine). No cross-reaction was observed to the pyridinoline, 2'-deoxypyridinoline possessing "pyridinium ring" and derived from collagen cross-links, structurally unrelated cysteic acid and taurine, nor core structure of 2-aminopyridine. The antiserum specifically recognized the molecules derived from the elastin cross-links. Using the ELISA assay system with antisera and amino acids analysis, 10 micrograms of desmosine were extracted from 1.0 mg of the hydrolysate of commercial elastin.
Watanabe
T
T
Cell Biology Research Laboratory, School of Medicine, Tokai University, Kanagawa, Japan.
Matsuki
H
H
Ogawa
T
T
Kawanishi
Y
Y
Kasuga
H
H
D000596:Amino Acids / Q000276:immunology; D000818:Animals; D000906:Antibodies; D000918:Antibody Specificity; D003429:Cross Reactions; D003895:Desmosine / Q000276:immunology* / Q000302:isolation & purification; D004549:Elastin / Q000302:isolation & purification; D004797:Enzyme-Linked Immunosorbent Assay; D011817:Rabbits
D000596:Amino Acids; D000906:Antibodies; D003895:Desmosine; C015484:pyridinoline; D004549:Elastin