Detailed Information on Publication Record
2002
Cytochrome c forms complexes and is partly reduced at interaction with GPI-anchored phosphatase
DADÁK, Vladimír, Oldřich JANICZEK and Oldřich VRÁNABasic 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
Článek v odborném periodiku
Confidentiality degree
není předmětem státního či obchodního tajemství
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
Změněno: 5/12/2002 08:43, doc. RNDr. Oldřich Janiczek, CSc.
V originále
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.
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.