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

Authors: Yoshii, K  Sugimoto, K  Tai, Y  Konishi, R  Tokuda, M 
Citation: Yoshii K, etal., Acta Med Okayama. 2000 Apr;54(2):57-65.
Pubmed: (View Article at PubMed) PMID:10806526

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.

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CRRD Object Information
CRRD ID: 2306913
Created: 2009-05-12
Species: All species
Last Modified: 2009-05-12
Status: ACTIVE



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