Dynamics of α-Hb chain binding to its chaperone AHSP depends on heme coordination and redox state.
Biochim Biophys Acta
; 1840(1): 277-87, 2014 Jan.
Article
en En
| MEDLINE
| ID: mdl-24060751
Palabras clave
AHSP; AHSP(WT); AHSP:α-Hb; Alpha-hemoglobin stabilizing protein (AHSP); Chaperone; Cyt b5; Erythropoiesis; GST; Hb; Heme hexacoordination; Hemoglobin; MetHb; Ngb; PBS; RBCs; ROS; alpha hemoglobin-stabilizing protein; complex formed between WT α-Hb chain and recombinant human wild type AHSP; ferric heme; glutathione S-transferase; hemin; human adult hemoglobin; neuroglobin; oxidized Hb; phosphate-buffered saline; reactive oxygen species; recombinant human wild type AHSP with an N-terminal Gly-Pro-Leu-Gly-Ser peptide; recombinant soluble domain of human membrane-bound cytochrome b5; red blood cells
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Hemoglobina A
/
Proteínas Sanguíneas
/
Chaperonas Moleculares
/
Hemo
Límite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
2014
Tipo del documento:
Article