JaLCDOI 10.18926/AMO/32286
フルテキストURL fulltext.pdf
著者 Yoshii, Kenji| Sugimoto, Katsuyoshi| Tai, Yuji| Konishi, Ryoji| Tokuda, Masaaki|
抄録 <p>Annexin was purified from rat liver mitochondria to an apparent homogeneity with a molecular weight of 35 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified mitochondrial annexin (AXmito) was identified as annexin I by an immunoblot analysis using anti-annexin I antibody. The inhibitory effect of AXmito I on porcine pancreatic phospholipase A2 activity was as potent as that of bovine lung annexin I. The presence of annexin I in mitochondria was confirmed by an electron-microscopic study. AXmito I was shown to be phosphorylated by intrinsic protein tyrosine kinases on its tyrosine residues. This annexin was also phosphorylated by protein kinase C.</p>
キーワード annexin mitochondria protein tyrosine kinases protein kinase C Phospholipase A2
Amo Type Article
発行日 2000-04
出版物タイトル Acta Medica Okayama
54巻
2号
出版者 Okayama University Medical School
開始ページ 57
終了ページ 65
ISSN 0386-300X
NCID AA00508441
資料タイプ 学術雑誌論文
言語 English
論文のバージョン publisher
査読 有り
PubMed ID 10806526
Web of Sience KeyUT 000086735900002