IMMUNOCHEMICAL APPROACH TO CHARACTERIZE POSTTRANSLATIONAL MODIFICATION OF SERUM-ALBUMIN USING ANTI-GLUTARALDEHYDE-TREATED SERUM-ALBUMIN ANTIBODIES

Polyclonal antibodies against glutaraldehyde-treated rabbit serum albu min (pHSA) and human serum albumin (pHSA) were prepared from rabbit an d mouse, respectively, Anti-pRSA antibody had the structural determina nt depending on the polymerization process of RSA and showed only a we ak cross-reactivity with the other glutaraldehyde-treated albumins. An ti-pHSA antibody (after adsorption of anti-HSA antibody) recognized on ly pHSA, but not HSA and the other treated albumins, The cross-reactiv ity of those antibodies was examined with albumins treated by other me thods such as modification of glucose and fructose, carbodiimide, and transglutaminase. Among them, RSA and HSA modified with glucose and fr uctose had an affinity for each antibody and the reactivity depended o n the extent of formation of the polymerized albumin, The result sugge sts that functional groups involved in cross-linking of albumin are im portant for formation of the cross-reactivity with the antibody and th at a definite structure immunochemically similar to glutaraldehyde-tre ated albumin could be formed by the Maillard reaction.