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Post by Max on Jun 12, 2005 4:09:18 GMT -5
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Post by Max on Jun 12, 2005 4:09:36 GMT -5
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Post by Max on Jun 12, 2005 4:10:05 GMT -5
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Post by Max on Jun 12, 2005 4:10:33 GMT -5
c
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Post by Max on Jun 12, 2005 4:11:02 GMT -5
References:
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Post by Max on Jun 12, 2005 15:50:58 GMT -5
Biochim Biophys Acta. 2002 Feb 15;1570(1):9-18. Related Articles, Links
Cytochrome c forms complexes and is partly reduced at interaction with GPI-anchored alkaline phosphatase.
Dadak V, Janiczek O, Vrana O.
Department of Biochemistry, Faculty of Science, Masaryk University, 61137, Brno, Czech Republic.
Cytochrome (cyt) c forms complexes, undergoes a conformational change and becomes partly reduced at interaction with membrane anchored alkaline phosphatase (AP), a glycoprotein which is released into the body fluid in forms differing in hydrophobicity. The proportion of products formed in the mixtures depends on pH, ionic strength, temperature and the buffer composition. The reaction terminates in an equilibrium between cyt c(FeII) and other cyt c conformers. Optimal conditions for the rate of the reaction are 100 mM glycine/NaOH, pH 9.7-9.9, at which 68-74% of cyt c is found in the reduced state. The interaction affects compactness of the haem cleft as shown by changes induced in CD spectra of the Soret region and changes in optical characteristics of phenylalanine, tyrosine and tryptophan residues. Differential scanning calorimetry of AP+cyt c mixtures revealed a creation of at least two types of complexes. A complex formed by non-coulombic binding prevails at substoichiometric AP/cyt c ratios, at higher ratios more electrostatic attraction is involved and at 1:1 molar ratio an apparent complexity of binding forces occurs. The rapid phase of the cyt c(FeII) formation depends on the presence of the hydrophobic alkylacylphosphoinositol (glycosylphosphatidylinositol) moiety, the protein part of the enzyme participates in an electrostatic and much slower phase of cyt c(FeII) creation. The results show that non-coulombic interaction may participate at interaction of cyt c with cellular proteins.
PMID: 11960683 [PubMed - indexed for MEDLINE]
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Post by Max on Jul 19, 2005 10:24:40 GMT -5
Cell Death Differ. 2005 Jul 8; [Epub ahead of print] Related Articles, Links
Early mitochondrial alterations in ATRA-induced cell death.
Schmidt-Mende J, Gogvadze V, Hellstrom-Lindberg E, Zhivotovsky B.
[1] 1Institute of Environmental Medicine, Division of Toxicology, Karolinska Institutet, Box 210, Stockholm SE-171 77, Sweden [2] 2Department of Medicine, Division of Hematology, Karolinska University Hospital Huddinge, Stockholm SE-141 86, Sweden.
All-trans retinoic acid (ATRA) induces differentiation and subsequent apoptosis in a variety of cell lines. Using the myeloid cell line P39, we show that ATRA disturbs mitochondrial functional activity long before any detectable signs of apoptosis occur. These early changes include diminished mitochondrial oxygen consumption, decreased calcium uptake by mitochondria and as a result, a lower mitochondrial matrix calcium concentration. Granulocyte colony-stimulating factor (G-CSF) increases mitochondrial respiration and calcium accumulation capacity and subsequently blocks ATRA-induced apoptosis. Nifedipine, a plasma membrane calcium channel blocker, inhibits apoptosis-related changes, such as the loss of the mitochondrial membrane potential and activation of caspases. Thus, the properties of ATRA and G-CSF to modulate mitochondrial respiration and intracellular calcium control are novel findings, which give insight into their precise molecular mode of action.Cell Death and Differentiation advance online publication, 8 July 2005; doi:10.1038/sj.cdd.4401715.
PMID: 16003389 [PubMed - as supplied by publisher]
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