Human erythrocyte membrane band 3 protein influences hemoglobin cooperativity. Possible effect on oxygen transport

Hemoglobin function can be modulated by the red cell membrane but some mechanistic details are incomplete. For example, the 43-kDa chymotryptic fragment of the cytoplasmic portion of red cell membrane Band 3 protein and its corresponding N-terminal 11-residue synthetic peptide lower the oxygen affin...

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Veröffentlicht in:	The Journal of biological chemistry 2003-10, Vol.278 (41), p.39565-39571
Hauptverfasser:	Zhang, Yuxun, Manning, Lois R, Falcone, Jill, Platt, Orah, Manning, James M
Format:	Artikel
Sprache:	eng
Schlagworte:	2,3-Diphosphoglycerate - pharmacology Amino Acid Sequence Anion Exchange Protein 1, Erythrocyte - chemistry Anion Exchange Protein 1, Erythrocyte - genetics Anion Exchange Protein 1, Erythrocyte - metabolism Biological Transport, Active Chlorides - pharmacology Erythrocyte Membrane - metabolism Hemoglobin A - metabolism Hemoglobin, Sickle - metabolism Humans In Vitro Techniques Kinetics Oxygen - metabolism Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism
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Zusammenfassung:	Hemoglobin function can be modulated by the red cell membrane but some mechanistic details are incomplete. For example, the 43-kDa chymotryptic fragment of the cytoplasmic portion of red cell membrane Band 3 protein and its corresponding N-terminal 11-residue synthetic peptide lower the oxygen affinity of hemoglobin but effects on cooperativity are unclear. Using highly purified preparations, we also find a lowered Hill coefficient (n values
ISSN:	0021-9258
DOI:	10.1074/jbc.M303352200