Polymorphisms in human soluble epoxide hydrolase: Effects on enzyme activity, enzyme stability, and quaternary structure

Archives of Biochemistry and Biophysics

Volumn 427, Issue 2, 2004, Pages 164-169

  Srivastava, Punit K ^a   Sharma, Vikas K ^a   Kalonia, Davendra S ^a   Grant, David F ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

Dimer; Epoxide hydrolase; Monomer; Phosphatase; Polymorphism; SNP; Stability

Indexed keywords

ARGININE; CYSTEINE; EPOXIDE HYDROLASE; GLYCINE; LYSINE; TYROSINE;

ALLELE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MUTANT; DIMERIZATION; DNA POLYMORPHISM; ENZYME ACTIVITY; GEL PERMEATION CHROMATOGRAPHY; GENE FREQUENCY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY;

AMINO ACID SUBSTITUTION; ENZYME ACTIVATION; ENZYME STABILITY; EPOXIDE HYDROLASES; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTATION; POLYMORPHISM, GENETIC; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP;

FELIS CATUS;

EID: 2942579253     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.abb.2004.05.003     Document Type: Article

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