| 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 |
Leucine Dehydrogenaseを共役させたヒトAminopeptidaseの定量的活性染色法 |
|
言語 |
ja |
| 言語 |
|
|
言語 |
jpn |
| キーワード |
|
|
主題 |
leucine aminopeptidase |
| キーワード |
|
|
主題 |
arylamidase |
| キーワード |
|
|
主題 |
cystyl aminopeptidase |
| キーワード |
|
|
主題 |
L-leucinamide |
| キーワード |
|
|
主題 |
leucine dehydrogenase |
| 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 |
神田, 進司
真鍋, 満久
須藤, 加代子
菅野, 剛史
柴田, 秀司
|
| 書誌情報 |
生物物理化学
巻 25,
号 3,
p. 167-171,
発行日 1981-12-21
|
| 出版者 |
|
|
出版者 |
日本電気泳動学会 |
| 権利 |
|
|
権利情報 |
日本電気泳動学会 |
| 抄録 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
An electrophoretic separation and a quantitative staining method for leucine aminopeptidase, arylamidase and cystyl aminopeptidase were described. L-Leucinamide was used as a substrate for the aminopeptidases electrophoretically separated, and the liberated L-leucine was oxidized by leucine dehydrogenase and NAD+. The activity bands were visualized by tetrazolium salt (MTT) as a final hydrogen acceptor. Arylamidase and cystyl aminopeptidase were stained in the area of pre α1-and between α1 andα2-globulin position, respectively. The leucine aminopeptidase was samely stained in the area of preβ-globulin. Employing this method, it was possible to determine the activity of each aminopeptidase with satisfactory accuracy and reproducibility. Furthermore, this method would be useful to the analysis of enzymological properties of aminopeptidases because of its availability to other peptides, such as L-leucylglycine and L-leucyl-L-leucine, as substrate. |
| 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.25.167 |
| 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 |
Seibutubuturi25_3-167.pdf (3.6 MB)
