The monoclonal antibody 1F6 identifies a pH-dependent conformational change in the hydrophilic NH2 terminus of NhaA Na+/H+ antiporter of Escherichia coli

Journal of Biological Chemistry

Volumn 275, Issue 7, 2000, Pages 4734-4742

  Venturi, Miro ^a   Rimon, Abraham ^b   Gerchman, Yoram ^b   Hunte, Carola ^a   Padan, Etana ^b   Michel, Harmut ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTER; EPITOPE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1F6; N ETHYLMALEIMIDE; TRYPSIN; UNCLASSIFIED DRUG;

ACIDITY; ALKALINITY; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANTIGEN BINDING; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; EPITOPE MAPPING; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; HYDROPHOBICITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; BLOTTING, WESTERN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SODIUM-HYDROGEN ANTIPORTER;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0034681398     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.7.4734     Document Type: Article

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