Characterization of leukocyte glucose 6-phosphate dehydrogenase in Sardinian mutants.

Publisher Website
Google Scholar
Abstract
The properties of the mutant glucose 6-phosphate dehydrogenase (G-6-PD) from the leukocytes of 54 subjects belonging to 28 families from different parts of Sardinia were studied. Studies with both crude and purified preparations of the enzyme showed that the mutant enzyme differs from the normal on the basis of the optimal pH activity, affinity for G-6-P and nicotinamide adenine dinucleotide phosphate (NADP), electrophoretic mobility, heat stability, NADP glycohydrolase (NADPase)-induced inactivation, and protection afforded by NADP. On the other hand, the sedimentation in the linear sucrose density gradient is similar to normal. These findings are discussed with respect to the mutation characteristics of the erythrocyte and leukocyte G-6-PD.