@article{oai:hama-med.repo.nii.ac.jp:00002395,
 author = {須藤, 加代子 and 前川, 真人 and 菅野, 剛史},
 issue = {3},
 journal = {生物物理化学},
 month = {May},
 note = {Anti-native lactate dehydrogenase (LD) A4 and B4 antibodies were prepared from white male rabbits. Binding affinities of these antibodies for the five isoenzymes of LD were quantitated. The equilibrium constants (Keq) showed, anti-A antibody> anti-B antibody≒LD inhibitor (IgG)> anti-acetylated B antibody≧LD-linked-Ig. Anti-A antibody formed complexes with LD-A subunit and the complexes were precipitated. Anti-B antibody also formed complexes with LD-B subunit and the complexes were precipitated, however, formed soluble complexes without inhibiting LD activity by diluting the antibody. LD-A4 and B4 showed the strongest affinity from antibody to A and B subunit, respectively. On the other hand, LD-linked-Ig and anti-acetylated B antibody formed soluble complexes with LD isoenzymes without inhibiting LD activity, and showed the strongest affinity to LD-2,3 and LD-1,2,3 (almost the same affinity), respectively. From these results, both LD-linked-Ig and anti-acetylated B antibody demonstrated to recognize the structure of neither A nor B subunit.},
 pages = {223--228},
 title = {乳酸脱水素酵素に対する酵素結合性免疫グロブリンおよび抗サブユニット抗体の結合親和性},
 volume = {30},
 year = {1986}
}