| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2013-08-27 |
| タイトル |
|
|
タイトル |
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 |
|
言語 |
ja |
| 言語 |
|
|
言語 |
jpn |
| キーワード |
|
|
主題 |
soluble immune complexes |
| キーワード |
|
|
主題 |
anti-lactate dehydrogenase A subunit antibody |
| キーワード |
|
|
主題 |
Antilactate dehydrogenase B subunit antibody |
| キーワード |
|
|
主題 |
lactate dehydrogenase anomaly |
| キーワード |
|
|
主題 |
Equilibrium constant. |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 著者 |
須藤, 加代子
前川, 真人
菅野, 剛史
|
| 書誌情報 |
生物物理化学
巻 30,
号 3,
p. 223-228,
発行日 1986-05-31
|
| 出版者 |
|
|
出版者 |
日本電気泳動学会 |
| 権利 |
|
|
権利情報 |
日本電気永動学会 |
| 抄録 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
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. |
| ISSN |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
00319082 |
| EISSN |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
13499785 |
| 出版社DOI |
|
|
関連タイプ |
isIdenticalTo |
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
10.2198/sbk.30.223 |
| 著者版フラグ |
|
|
出版タイプ |
VoR |
|
出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
Seibutubuturi30_3-223.pdf (5.3 MB)
