An analysis of suppressor mutations suggests that the two halves of the lactose permease function in a symmetrical manner

Journal of Biological Chemistry

Volumn 272, Issue 42, 1997, Pages 26110-26116

  Pazdernik, Nanette J ^a   Cain, Shane M ^a   Brooker, Robert J ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LACTOSE PERMEASE; LEUCINE; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; MUTATION; NONHUMAN; PRIORITY JOURNAL;

BIOLOGICAL TRANSPORT; ESCHERICHIA COLI PROTEINS; GENES, SUPPRESSOR; KINETICS; LACTOSE; MEMBRANE TRANSPORT PROTEINS; MONOSACCHARIDE TRANSPORT PROTEINS; MUTATION; SYMPORTERS;

EID: 0030724004     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.42.26110     Document Type: Article

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