Temperature-nearly-independent binding constant in several biochemical systems: The underlying entropy-driven binding mechanism and its practical significance

Biochemical Pharmacology

Volumn 51, Issue 6, 1996, Pages 723-729

  Miklavc, Adolf ^a  

^a NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

Author keywords

Acetylcholinesterase; Adrenergic receptor blockers; Binding constant; Binding sites; Cholinesterase inhibitors; NADH dehydrogenase; Temperature nearly independent

Indexed keywords

ACETYLCHOLINESTERASE; ALCOHOL DEHYDROGENASE; BETA ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR BLOCKING AGENT; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CARAZOLOL; CHOLINESTERASE INHIBITOR; DOPAMINE; DOPAMINE RECEPTOR BLOCKING AGENT; DOPAMINE RECEPTOR STIMULATING AGENT; HALOPERIDOL; ISOPRENALINE; LIVER ENZYME; NORADRENALIN; OCTOPINE DEHYDROGENASE; PRACTOLOL; PROPRANOLOL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

ARTICLE; BINDING KINETICS; BINDING SITE; BIOCHEMISTRY; DISSOCIATION CONSTANT; ENTHALPY; ENTROPY; ENZYME BINDING; HORSE; HYDROPHOBICITY; MODEL; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; TEMPERATURE; THERMODYNAMICS;

ACETYLCHOLINESTERASE; ADRENERGIC BETA-ANTAGONISTS; ALCOHOL DEHYDROGENASE; AMINO ACID OXIDOREDUCTASES; ANIMALS; BENZOQUINONES; BINDING SITES; CHEMISTRY, PHYSICAL; CHOLINESTERASE INHIBITORS; HORSES; KINETICS; LIVER; NAD; QUATERNARY AMMONIUM COMPOUNDS; TEMPERATURE;

EID: 0029863526     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(95)02161-2     Document Type: Note

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