Watanabe T, Nakasaki H, Mitomi T, Kamijou A, Matsuki H, Kasuga H
Laboratories for Structure and Function, Tokai University School of Medicine, Kanagawa, Japan.
Tokai J Exp Clin Med. 1994 Dec;19(3-6):103-7.
Eight mouse IgG1 monoclonal anti-Adriamycin antibodies were produced in culture and in ascites in BALB/c nude mice. The binding constant and specificity was measured by an inhibition ELISA method. The assay was an indirect method using horseradish peroxidase-labeled goat Fab' antibody and 2mM ABTS (2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) containing 2.5 mM H2O2 as a color reaction reagent. The binding constant of the antibodies was 10(6) to 10(8) M-1. The antibodies possessed different specificities and affinities to the adriamycin. Though adriamycin is a low molecular weight (M.W. 579.99) hapten antigen, it possesses several epitopes as antigenic determinant sites. The antigenic epitopes of the adriamycin, which until recently were unknown, were analyzed by the monoclonal antibodies.
在培养物中以及BALB/c裸鼠的腹水中产生了8种小鼠IgG1单克隆抗阿霉素抗体。通过抑制ELISA法测定结合常数和特异性。该测定是一种间接方法，使用辣根过氧化物酶标记的山羊Fab'抗体和含有2.5 mM H2O2的2 mM ABTS（2,2'-叠氮基双（3-乙基苯并噻唑啉-6-磺酸）作为显色反应试剂。抗体的结合常数为10(6)至10(8) M-1。这些抗体对阿霉素具有不同的特异性和亲和力。尽管阿霉素是一种低分子量（分子量579.99）的半抗原，但它具有几个作为抗原决定簇位点的表位。直到最近还未知的阿霉素的抗原表位通过单克隆抗体进行了分析。
