Title : The interaction of acrylamide with glyceraldehyde-3-phosphate dehydrogenase. Structural modifications in the enzyme studied by fluorescence techniques.

Pub. Date : 1990 Jun

PMID : 2367567






4 Functional Relationships(s)
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1 When GPDH containing about 1 mol NAD per mol of tetramer is incubated with acrylamide (0.01-0.1 M), the tryptophan emission of GPDH, initially quenched by acrylamide, slowly increases to a value exceeding that recorded before the addition of acrylamide. NAD glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus
2 When GPDH containing about 1 mol NAD per mol of tetramer is incubated with acrylamide (0.01-0.1 M), the tryptophan emission of GPDH, initially quenched by acrylamide, slowly increases to a value exceeding that recorded before the addition of acrylamide. NAD glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus
3 This effect is not observed in apoenzyme solutions, indicating that the enhancement of fluorescence results from the dissociation of some NAD from the acrylamide treated GPDH. NAD glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus
4 Acrylamide inactivates GPDH but 1 mM NAD protects the enzyme from inactivation. NAD glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus