Purification, identification and phosphorylation of annexin I from rat liver mitochondria

Autor:	Yoshii, Kenji, Sugimoto, Katsuyoshi, Tai, Yuji, Konishi, Ryoji, Tokuda, Masaaki
Rok vydání:	2000
Předmět:	Mitochondria Liver protein tyrosine kinases Protein-Tyrosine Kinases Phospholipases A Rats mitochondria annexin Phospholipases A2 Phospholipase A2 Animals Electrophoresis Polyacrylamide Gel Phosphorylation Microscopy Immunoelectron Pancreas Protein Kinase C Annexin A1
Zdroj:	Acta medica Okayama. 54(2)
ISSN:	0386-300X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::42ee0fc75f7523de1e5756f76ab68b6f https://pubmed.ncbi.nlm.nih.gov/10806526 Zobrazit plný text záznamu