The C-terminal cytoplasmic portion of the NhaP2 cation-proton antiporter from Vibrio cholerae affects its activity and substrate affinity

Molecular and Cellular Biochemistry

Volumn 389, Issue 1-2, 2014, Pages 51-58

  Wiens, Evan J ^a   Winogrodzki, Judith L ^a   Resch, Craig T ^a   Orriss, George L ^a   Stetefeld, Jörg ^a   Dibrov, Pavel ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

Author keywords

cation proton antiporter; Deletion analysis; Soluble domain; Vibrio cholerae

Indexed keywords

ANTIPORTER; NHAP2 PROTEIN; POTASSIUM ION; SODIUM ION; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM CULTURE; CELL FRACTIONATION; CHROMOSOME DELETION; CONTROLLED STUDY; CYTOPLASM; ESCHERICHIA COLI; IMMUNODETECTION; MEMBRANE VESICLE; NONHUMAN; PH; PHENOTYPE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN DETERMINATION; SODIUM TRANSPORT; VIBRIO CHOLERAE; WESTERN BLOTTING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; VIBRIO CHOLERAE;

BACTERIAL PROTEINS; CATIONS; CLONING, MOLECULAR; CYTOPLASM; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; POTASSIUM; SODIUM; SODIUM-HYDROGEN ANTIPORTER; VIBRIO CHOLERAE;

EID: 84896548186     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-013-1926-x     Document Type: Article

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