DADÁK, Vladimír, Oldřich JANICZEK a Oldřich VRÁNA. Cytochrome c forms complexes and is partly reduced at interaction with GPI-anchored phosphatase. BBA : Biochimica et biophysica acta : international journal of biochemistry and biophysics. Amsterdam: Elsevier, 2002, roč. 2002, s. 9-17. ISSN 0304-4165.
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Základní údaje
Originální název Cytochrome c forms complexes and is partly reduced at interaction with GPI-anchored phosphatase
Autoři DADÁK, Vladimír, Oldřich JANICZEK a Oldřich VRÁNA.
Vydání BBA : Biochimica et biophysica acta : international journal of biochemistry and biophysics. Amsterdam, Elsevier, 2002, 0304-4165.
Další údaje
Typ výsledku Článek v odborném periodiku
Utajení není předmětem státního či obchodního tajemství
Impakt faktor Impact factor: 1.845
Organizační jednotka Přírodovědecká fakulta
Klíčová slova anglicky Cytochrome c; Cytochrome c complex; Aromatic amino acid; Alkaline phosphatase; Glycosylphosphatidylinositol anchor; Non/coulombic binding; Apoptosis
Štítky alkaline phosphatase, apoptosis, Aromatic amino acid, cytochrome c, Cytochrome c complex, Glycosylphosphatidylinositol anchor, Non/coulombic binding
Změnil Změnil: doc. RNDr. Oldřich Janiczek, CSc., učo 2578. Změněno: 5. 12. 2002 08:43.
Anotace
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.
Anotace anglicky
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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