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Volumn 408, Issue 2, 2002, Pages 295-304

The temperature dependence of activity and structure for the most prevalent mutant aldolase B associated with hereditary fructose intolerance

(3) Malay, Ali D a Procious, Sheri L b Tolan, Dean R a

a Boston University (United States)

b TUFTS UNIVERSITY (United States)

Author keywords

Carbohydrate; Circular dichroism spectroscopy; Enzyme kinetics; Genetic disease; Hydrodynamics; Inborn errors in metabolism; Liver metabolism; Quaternary structure; Sugar phosphate binding; Thermolability

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE;

ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME STRUCTURE; HEREDITARY FRUCTOSE INTOLERANCE; MUTATION; PRIORITY JOURNAL; TEMPERATURE; THERMOSTABILITY; ULTRAVIOLET RADIATION;

BINDING SITES; CIRCULAR DICHROISM; DIMERIZATION; ENZYME STABILITY; FRUCTOSE INTOLERANCE; FRUCTOSE-BISPHOSPHATE ALDOLASE; HUMANS; KINETICS; MUTATION; PHOSPHATES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; TEMPERATURE;

EID: 0036910881 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1016/S0003-9861(02)00546-5 Document Type: Article

Times cited : (19)

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