Three-state kinetic analysis of chinese hamster dihydrofolate reductase unfolding by guanidine hydrochloride

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1343, Issue 1, 1997, Pages 107-116

  Wu, Jia Wei ^a   Wang, Zhi Xin ^a   Zhou, Jun Mei ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Enzyme inactivation; Kinetic constant; Protein denaturation; Substrate protection; Unfolding intermediate

Indexed keywords

DIHYDROFOLATE REDUCTASE; GUANIDINE;

ANIMAL CELL; ARTICLE; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME SUBSTRATE; HAMSTER; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; CRICETINAE; CRICETULUS; ENZYME ACTIVATION; GUANIDINE; KINETICS; PROTEIN FOLDING; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 0031455351     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(97)00089-7     Document Type: Article

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