Purification and detailed study of two clinically different human glucose 6-phosphate dehydrogenase variants, G6PDPlymouth and G6PDMahidol: Evidence for defective protein folding as the basis of disease

Molecular Genetics and Metabolism

Volumn 93, Issue 1, 2008, Pages 44-53

  Huang, Yuxiang ^a   Choi, Mei Yee ^a   Au, Shannon Wing Ngor ^b   Au, Deborah Man Yee ^a   Lam, Veronica Min Sien ^a   Engel, Paul C ^c  

^a UNIVERSITY OF HONG KONG   (Hong Kong)

^b CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

^c UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Disease mutations; Enzyme stability; Glucose 6 phosphate dehydrogenase deficiency; Kinetic properties; Protein folding; Recombinant expression

Indexed keywords

GLUCOSE 6 PHOSPHATE DEHYDROGENASE;

ARTICLE; BACTERIAL CELL; CONTROLLED STUDY; ENZYME PURIFICATION; ESCHERICHIA COLI; GENE EXPRESSION; GENE MUTATION; GLUCOSE 6 PHOSPHATE DEHYDROGENASE DEFICIENCY; MOLECULAR DYNAMICS; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; STEADY STATE; TEMPERATURE; THERMOSTABILITY; WILD TYPE;

CHAPERONINS; GENE EXPRESSION; GLUCOSEPHOSPHATE DEHYDROGENASE; GLUCOSEPHOSPHATE DEHYDROGENASE DEFICIENCY; GROEL PROTEIN; GROES PROTEIN; HUMANS; MODELS, MOLECULAR; MUTANT PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; TEMPERATURE;

EID: 36849081934     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2007.08.122     Document Type: Article

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