Multiple unfolding states of glutathione transferase from Physa acuta (Gastropada: Physidae)

Biochemical and Biophysical Research Communications

Volumn 340, Issue 2, 2006, Pages 625-632

  Abdalla, Abdel Monem ^a   Hamed, Ragaa R ^a  

^a NATIONAL RESEARCH CENTRE   (Egypt)

Author keywords

Chromatography; Fluorescence; Folding; Glutathione transferase; Intermediates; Subunit interactions; Unfolding

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; GLUTATHIONE TRANSFERASE; GUANIDINE; UREA;

ACIDITY; ARTICLE; CONTROLLED STUDY; DENATURATION; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBUNIT; FLUORESCENCE ANALYSIS; ISOENZYME ANALYSIS; NONHUMAN; PHASE TRANSITION; PHYSA ACUTA; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN MODIFICATION; SNAIL; STRUCTURE ANALYSIS;

ANIMALS; ENZYME STABILITY; GASTROPODA; GLUTATHIONE TRANSFERASE; GUANIDINE; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; UREA;

GASTROPODA; PHYSA ACUTA; PHYSIDAE;

EID: 29644435021     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.12.048     Document Type: Article

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