The substrate recognition domain in the Na+/dicarboxylate and Na+/sulfate cotransporters is located in the carboxy-terminal portion of the protein

Biochimica et Biophysica Acta - Biomembranes

Volumn 1370, Issue 1, 1998, Pages 98-106

  Pajor, Ana M ^a   Sun, Ning ^a   Bai, Liqun ^a   Markovich, Daniel ^b   Sule, Patricia ^a  

^a UNIVERSITY OF ARIZONA COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

(Xenopus); Chimera; Dicarboxylate; Oocyte; Sodium; Sulfate

Indexed keywords

CARRIER PROTEIN; DICARBOXYLIC ACID; FLUFENAMIC ACID; FUROSEMIDE; SODIUM ION; SULFATE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHIMERA; CONTROLLED STUDY; ENZYME SPECIFICITY; MEMBRANE TRANSPORT; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN DOMAIN; XENOPUS LAEVIS;

ANIMALS; ANTIBODIES; BINDING SITES; BLOTTING, WESTERN; CARBOXYLIC ACIDS; CARRIER PROTEINS; CATION TRANSPORT PROTEINS; CATIONS; DICARBOXYLIC ACID TRANSPORTERS; ION TRANSPORT; KINETICS; MEMBRANE PROTEINS; OOCYTES; ORGANIC ANION TRANSPORTERS, SODIUM-DEPENDENT; RECOMBINATION, GENETIC; SODIUM; SUBSTRATE SPECIFICITY; SULFATES; SYMPORTERS; XENOPUS;

ANIMALIA; XENOPUS LAEVIS;

EID: 0032489638     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(97)00249-6     Document Type: Article

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