Flufenamic acid senses conformation and asymmetry of human erythrocyte band 3 anion transport protein.
about
35Cl nuclear magnetic resonance line broadening shows that eosin-5-maleimide does not block the external anion access channel of band 3.The noncompetitive inhibitor WW781 senses changes in erythrocyte anion exchanger (AE1) transport site conformation and substrate binding.Characterization of oxalate transport by the human erythrocyte band 3 protein.Critical amino acid residues involved in the electrogenic sodium-bicarbonate cotransporter kNBC1-mediated transport.Effects of external pH on substrate binding and on the inward chloride translocation rate constant of band 3.Effects of external pH on binding of external sulfate, 4.4-dinitro-stilbene-2,2'-disulfonate (DNDS), and chloride to the band 3 anion exchange protein.
P2860
Flufenamic acid senses conformation and asymmetry of human erythrocyte band 3 anion transport protein.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh-hant
name
Flufenamic acid senses conform ...... and 3 anion transport protein.
@en
Flufenamic acid senses conform ...... and 3 anion transport protein.
@nl
type
label
Flufenamic acid senses conform ...... and 3 anion transport protein.
@en
Flufenamic acid senses conform ...... and 3 anion transport protein.
@nl
prefLabel
Flufenamic acid senses conform ...... and 3 anion transport protein.
@en
Flufenamic acid senses conform ...... and 3 anion transport protein.
@nl
P2093
P2860
P1476
Flufenamic acid senses conform ...... and 3 anion transport protein.
@en
P2093
P2860
P304
P356
10.1152/AJPCELL.1989.257.2.C277
P407
P433
P577
1989-08-01T00:00:00Z