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At least 19 recordsLinked to original sources
PubMed1987

[Lactate dehydrogenase, glucosephosphate dehydrogenase, glutathione reductase and adenosine triphosphatase activities in the erythrocytes of patients with acute viral hepatitis].

Some indices of erythrocyte metabolism (EM): activity of lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PD), glutathione reductase (GR) and common adenosinetriphosphatase (ATPase) activity were studied in 102 patients with acute viral hepatitis (AVH). The suppression of erythrocyte enzymatic activity (EE) was revealed. It was most noticeable at the peak of average and severe AVH. In a decrease of jaundice and during reconvalescence G-6-PD, GR and ATPase activity reduced up to the control level. The suppression of LDH activity was more noticeable, maintained at discharge and was of prognostic value in investigation at early periods of disease in cases of prolonged reconvalescence. Changes in EE activity showed correlation with indices of liver function (levels of certain bilirubin fractions and transaminase activity). In cases of developing deficiency of erythrocyte G-6-PD activity there was a high correlation between a degree of cytolysis and the suppression of erythrocyte LDH activity. The importance of erythrocyte metabolic derangements revealed in AVH pathogenesis was discussed.

Acute Disease↗
PubMed1999

Effect of artemether on phosphorylase, lactate dehydrogenase, adenosine triphosphatase, and glucosephosphate dehydrogenase of Schistosoma japonicum harbored in mice.

AIM: To study the effect of artemether (Art) on phosphorylase (PP), lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PDH), and adenosine triphosphatase (ATPase) of S japonicum. METHODS: Mice infected with S. japonicum cercariae for 32-38 d were treated i.g. with Art 100-300 mg.kg-1 and killed 24-72 h after treatment for collection of schistosomes. The activities of PP, LDH, and G-6-PDH were measured by the formation of NADH or NADPH. The activity of ATPase was measured by the rate of release of inorganic phosphate (Pi) from ATP at 37 degrees C. RESULTS: After infected mice were treated i.g. with Art 300 mg.kg-1 for 24-48 h, the activities of total PP and PPa (active form) increased markedly in both male and female worms, while PPb (inactive form) showed no or only a slight increase. At 24-72 h after the above-mentioned mice were treated i.g. with Art 100-300 mg.kg-1, the inhibitory rates of LDH and G-6-PDH were 9%-59% (male) and 41%-75% (female) as well as 22%-42% (male) and 74%-89% (female), respectively. When Art 300 mg.kg-1 was given to infected mice for 24 h, only the activity of Mg(2+)-ATPase showed marked inhibition in both male and female worms. At 48 h, the Ca(2+)-ATPase, Mg(2+)-ATPase, and Na(+)-K(+)-ATPase were all inhibited, the inhibitory rates of 17% (male) and 19% (female), 32% (male) and 48% (female) as well as 29% (male) and 44% (female), respectively. CONCLUSION: In schistosomes, the increase in the activity of AMP-independent PPa induced by Art may enhance the decomposition of glycogen and the inhibition of LDH by Art could reduce the formation of lactate. Moreover, Art exerts a potent inhibition on the G-6-PDH activity of the female S japonicum.

Adenosine Triphosphatases↗
PubMedDate not supplied

[Kinetic properties of partially purified glucosephosphate dehydrogenase of human erythrocytes].

Partially purified glucose-6-phosphate dehydrogenase was isolated from small amounts of human erythrocytes (15-20 ml). The Km value for glucose-6-phosphate was 35.0 +/- 3.0 micronM, the Km for NADP was 4.27 +/- 0.3 micronM. The optimal activity of the enzyme was at pH 9.0. Glucose-6-phosphate dehydrogenase, dialyzed in presence of 1-10(-5) M NADP, had critical temperature about 52 degrees within 10 min of incubation; without NADP it was at 45 degrees. The method for isolation and purification of the enzyme was modified.

Adult↗