Ala-504 is a determinant of substrate binding affinity in the mouse Na+/dicarboxylate cotransporter

Biochimica et Biophysica Acta - Biomembranes

Volumn 1758, Issue 6, 2006, Pages 781-788

  Oshiro, Naomi ^a   Pajor, Ana M ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

Author keywords

Adipate; NaDC1; Sodium; Substrate specificity; Succinate; Xenopus oocytes

Indexed keywords

ADIPIC ACID; ALANINE; COTRANSPORTER; GLUTARIC ACID; SERINE; SODIUM DICARBOXYLATE COTRANSPORTER; SUCCINIC ACID; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL MEMBRANE TRANSPORT; CONTROLLED STUDY; ELECTROPHYSIOLOGY; FEMALE; NONHUMAN; NUCLEOTIDE SEQUENCE; OOCYTE; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SODIUM TRANSPORT; VOLTAGE CLAMP; XENOPUS LAEVIS;

ALANINE; ANIMALS; DICARBOXYLIC ACID TRANSPORTERS; MICE; MUTAGENESIS, SITE-DIRECTED; SUBSTRATE SPECIFICITY; XENOPUS;

ORYCTOLAGUS CUNICULUS;

EID: 33746051327     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.05.005     Document Type: Article

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