DADÁK, Vladimír, Oldřich JANICZEK and Oldřich VRÁNA. Cytochrome c forms complexes and is partly reduced at interaction with GPI-anchored phosphatase. Online. BBA : Biochimica et biophysica acta : international journal of biochemistry and biophysics. Amsterdam: Elsevier, 2002, vol. 2002, p. 9-17. ISSN 0304-4165. [citováno 2024-04-24]
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Basic information
Original name Cytochrome c forms complexes and is partly reduced at interaction with GPI-anchored phosphatase
Authors DADÁK, Vladimír, Oldřich JANICZEK and Oldřich VRÁNA
Edition BBA : Biochimica et biophysica acta : international journal of biochemistry and biophysics. Amsterdam, Elsevier, 2002, 0304-4165.
Other information
Type of outcome Article in a journal
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 1.845
Organization unit Faculty of Science
Keywords in English Cytochrome c; Cytochrome c complex; Aromatic amino acid; Alkaline phosphatase; Glycosylphosphatidylinositol anchor; Non/coulombic binding; Apoptosis
Tags alkaline phosphatase, apoptosis, Aromatic amino acid, cytochrome c, Cytochrome c complex, Glycosylphosphatidylinositol anchor, Non/coulombic binding
Changed by Changed by: doc. RNDr. Oldřich Janiczek, CSc., učo 2578. Changed: 5/12/2002 08:43.
Abstract
Cytochrome c forms complexes, undergoes a conformational change and becomes partly reduced at interaction with membrane anchored alkaline phosphatase, 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 results show that non/coulombic interaction may participate at interaction of cyt c with cellular proteins.
Abstract (in English)
Cytochrome c forms complexes, undergoes a conformational change and becomes partly reduced at interaction with membrane anchored alkaline phosphatase, 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 results show that non/coulombic interaction may participate at interaction of cyt c with cellular proteins.
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