Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein.
Biochim Biophys Acta
; 985(3): 355-8, 1989 Nov 03.
Article
em En
| MEDLINE
| ID: mdl-2508756
ABSTRACT
After functional expression of mouse erythroid band 3 by cRNA microinjection into Xenopus oocytes, 36Cl- efflux is irreversibly inhibited by H2DIDS. When a cRNA is injected that is derived from a cDNA in which the nucleotides encoding for lysine-558 were replaced by nucleotides encoding for asparagine, transport and inhibition of transport by H2DIDS still occur. However, when measured under conditions where no intramolecular crosslinking takes place the inhibition by H2DIDS is no longer irreversible. This indicates that thiourea bond formation between H2DIDS and band 3 takes place at Lys-558.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ácido 4-Acetamido-4'-isotiocianatostilbeno-2,2'-dissulfônico
/
Estilbenos
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Proteína 1 de Troca de Ânion do Eritrócito
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Ácido 4,4'-Di-Isotiocianoestilbeno-2,2'-Dissulfônico
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Lisina
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Mutação
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1989
Tipo de documento:
Article