title: Derivative spectrophotometry of dimer and monomer of enolase.
abstract: 1. SDS causes significant polar exposure of aromatic amino acids of enolase. The alpha-helix content remains unchanged. The enzyme lost all its activity. 2. The presence of 1 M K Br in enzyme solution results in a smaller increase of polarity of aromatic amino acids residues environment. The amount of alpha-helix does not decrease in comparison to native enzyme. Enzyme lost nearly 80% of its initial activity. 3. The extreme pH values and the presence of 6 M Gnd.HCl influence the whole structure of enolase. It is accompanied by a large polar shift of aromatic amino acids and significant decrease of alpha-helix content of the protein.
authors.affiliation: Department of Biochemistry, Medical School, Wrocław, Poland.
authors.forename: E
authors.initials: E
authors.lastname: Kulig
authors.forename: M
authors.initials: M
authors.lastname: Wolny
mesh_terms: D000818:Animals; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology*; D010751:Phosphopyruvate Hydratase / Q000302:isolation & purification / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D013552:Swine
chemical_list: D046911:Macromolecular Substances; D010751:Phosphopyruvate Hydratase