Equilibrium unfolding studies of the rat liver methionine adenosyltransferase III, a dimeric enzyme with intersubunit active sites

Biochemical Journal

Volumn 361, Issue 2, 2002, Pages 307-315

  Gasset, María ^a   Alfonso, Carlos ^a   Neira, José L ^a   Rivas, Germán ^a   Pajares, María A ^a  

^a INSTITUTO DE INVESTIGACIONES BIOMÉDICAS ALBERTO SOLS   (Spain)

Author keywords

Methionine metabolism; Monomeric intermediate; S adenosylmethionine

Indexed keywords

BIODIVERSITY; BIOLOGICAL ORGANS; DIMERS; FREE ENERGY; SEDIMENTATION; SIZE EXCLUSION CHROMATOGRAPHY;

THERMODYNAMICAL PARAMETERE;

ENZYMES;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; DIMER; LIVER ENZYME; METHIONINE ADENOSYLTRANSFERASE; UREA;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISSOCIATION; ENERGY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; GEL PERMEATION CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; RAT; THERMODYNAMICS; ULTRACENTRIFUGATION;

ANILINO NAPHTHALENESULFONATES; ANIMALS; BINDING SITES; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; DIMERIZATION; FLUORESCENT DYES; LIVER; METHIONINE ADENOSYLTRANSFERASE; PROTEIN DENATURATION; PROTEIN FOLDING; RATS; SPECTROMETRY, FLUORESCENCE; ULTRACENTRIFUGATION;

EID: 0037081777     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3610307     Document Type: Article

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