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1.
Activity of glucose 6-phosphate dehydrogenase (D-glucose 6-phosphate:NADP oxidoreductase, EC 1.1.1.49 [EC] ) preparation from sweet potatoroot tissue was markedly altered in the presence of variousions. Cations or anions were effective in the following order:Na$, K$>Tris$>NH4$>Mg2$>Ca2$, or Cl>NO3,HPO42–>SO42–>HCO3. Activity was inhibitedat high concentrations of Ca2$, and HCO3,. In an investigationon the dependence of the activity on pH, two activity peakswere clearly observed at low ionic strength. Ionic strength altered both the Km and Vmax for glucose 6-phosphate(G6P). A Lineweaver-Burk plot for the enzyme, with respect toG6P, showed a bimodal nature at low ionic strength; suggestingnegative cooperativity. Deviation from linearity of the plotwas less with an increase in the ionic strength. 1 Present address: Institute of Applied Microbiology, Universityof Tokyo, Bunkyo-ku, Tokyo 113. (Received September 18, 1971; )  相似文献   

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Sedimentation behavior of sweet potato glucose 6-phosphate dehydrogenasewas studied using the sucrose density gradient centrifugation.The relative s value to s20, value of alcohol dehydrogenasewas determined to be about 6 in the absence of both NADP$ andglucose 6-phosphate. In the presence of NADP$, the enzyme wassedimented with a relative s value of about 9. The additionof glucose 6-phosphate did not affect the sedimentation behavior.When glucose 6-phosphate was added to the gradient medium containingNDAP$, the enzyme was sedimented with a relative s value ofabout 6 or 7, depending on the concentration of glucose 6-phosphate. 1 Present address: Institute of Applied Microbiology, Universityof Tokyo, Bunkyo-ku. Tokyo, Japan. (Received February 13, 1971; )  相似文献   

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NADPH2 and ATP competitively inhibit sweet potato glucose 6-phosphatedehydrogenase with NADP and glucose 6-phosphate (G6P), respectively.At pH 8.0, a Lineweaver-Burk plot of the reciprocal rate againstreciprocal G6P concentration was concave downwards in the presenceand absence of ATP, whereas a double reciprocal plot followedthe Michaelis-Menten relationship at pH 7.0, irrespective ofthe presence of ATP. Many of the other metabolic intermediatestested had no effects on the enzyme reaction. 1 This paper constitutes Part 96 of the Phytopathological Chemistryof Sweet Potato with Black Rot and Injury. 2 Present address: Institute of Applied Microbiology, Universityof Tokyo Bunkyo-ku, Tokyo 113. (Received October 20, 1971; )  相似文献   

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Electrophoretic analysis of glucose 6-phosphate dehydrogenase from liver and blood of rainbow trout revealed a complex series of bands, which could differ between fish. The partial interconvertible nature of these bands was demonstrated with enzyme that had been incompletely inactivated at pH 8.4. In a single population of 40 fish, a homozygote and a heterozygote for an electrophoretic variant allele were found. We suggest that G6PD in rainbow trout liver and blood is determined by two alleles at a single locus, with posttranslational modification responsible for the complex electrophoretic patterns seen. The basis for this variation appears to be NADH binding to the protein molecule. Another variant and other properties of the enzyme are described.Supported in part by the State of California Department of Mental Hygiene and by USPHS Grants GM-15253, HD-04612, HD-00315, HD-05615, and HL-15125. One of us (S.D.C.) was a Special Postdoctoral Fellow of NIAMD (No. 1F03AM-40, 329-01) during part of this work.  相似文献   

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Glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were separated and partially purified from glucose-grown cells of Lactobacillus casei. The enzymes had similar pH optima, thermosensitivity and molecular weights. They had different net charges and their pI values were 5.38 and 4.52, respectively. Histidine, arginine, lysine and cysteine residues were essential for the activity of G6PD, and all the above amino acids with the exception of lysine were required for 6PGD activity. Mg2+ activated 6PGD up to 15 mM concentration, above which it was inhibitory. It had no effect on G6PD activity. G6PD was specific for NADP+, but 6PGD showed some activity with NAD+ as the cofactor, although it was essentially NADP(+)-preferring. Both the enzymes, were inhibited by NADPH. 6PGD was also inhibited by its product, ribulose 5-phosphate. ATP inhibited 6PGD only at subsaturating concentrations of NADP+. The inhibition was sigmoidal in the absence of Mg2+ and hyperbolic in its presence.  相似文献   

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Sephadex G-200 gel-filtration of an enzymatic preparation fromsweet potato root tissue showed three activity peaks (I, IIand III) of 6-phosphogluconate dehydrogenase. Re-chromatographyof either Peak II or III produced two peaks corresponding toPeak II and III. Disc electrophoreses of the original preparation,Peak II, Peak III and the Peak II-like peak after re-chromatographygave idetical zymograms of the three isozymes which were notinterconvertible. 1 Present address: Institute of Applied Microbiology, Universityof Tokyo, Bunkyo-ku, Tokyo 113, Japan. (Received May 30, 1972; )  相似文献   

10.
We have evaluated the hypothesis of a negative association between glucose 6-phosphate dehydrogenase (G6PD) deficiency and cancer in a cohort of 481 Sardinian males with hematological malignancies. The frequency of G6PD deficiency in the patients was not different from the incidence in a group of 16,219 controls. The same conclusion resulted from the comparison of the frequency of expression of the GdB gene in 23 heterozygous women having a clonal hematologic disease and a control group of 37 healthy heterozygotes. Therefore at present there is no evidence that G6PD deficiency has a protective effect against development of hematologic neoplasms.  相似文献   

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Glucose 6-phosphate dehydrogenase produced by female Drosophila melanogaster differs from that of males in electrophoretic mobility, kinetics, and thermostability. The enzyme produced by pseudomales is intermediate in kinetics and stability, but resembles that of males in electrophoretic mobility. Stability and kinetics are affected by growth temperature in pseudomales.This research was supported by NIH grants, Nos. 5-T1-GM 216-06 and GM 12768-01 and NSF grants GB 4587 and GB 4824.  相似文献   

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《Translational oncology》2020,13(11):100842
Most cancer cells exacerbate the pentose phosphate pathway (PPP) to enhance biosynthetic precursors and antioxidant defenses. Metformin, which is used as a first-line oral drug for the treatment of type 2 diabetes, has been proposed to inhibit the malignant progression of different types of cancers. However, metformin has shown poor efficacy as single agent in several clinical trials. Thus, the aim of the present work was to investigate whether the pharmacological inhibition of G6PDH, the first and rate-limiting enzyme of the PPP, by 6-amino nicotinamide (6-AN) potentiates the antitumoral activity of metformin on different human melanoma cell lines. Our results showed that 6-AN has sensitizing properties to metformin cytotoxicity. The combination of metformin and 6-AN decreased glucose consumption and lactate production, altered the mitochondrial potential and redox balance, and thereby blocked melanoma cell progression, directing cells to apoptosis and necrosis. To our knowledge, this is the first study describing the effect of this combination. Future preclinical studies should be performed to reveal the biological relevance of this finding.  相似文献   

14.
A variant of glucose 6-phosphate dehydrogenase (G6PD) in Drosophila melanogaster shows different electrophoretic migration in males and females. In heterozygotes, the variant influences the migration of G6PD produced by both chromosomes. Mixing of homogenates of males and females changes migration of the female-produced enzyme, suggesting that a protein produced in males is capable of altering the variant G6PD molecule. The hypothetical protein is also present in pseudomales and intersexes produced by sex transformation genes.This research was supported by NIH grants # 5-T1-GM 216-06 and GM 12768-01 and NSF grants GB 4587 and GB 4824.  相似文献   

15.
Glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate:NADP+ 1-oxidoreductase, EC 1.1.1.49) was purified from rabbit erythrocytes. Initial velocity studies and product and dead-end inhibitor studies with this enzyme are consistent with a rapid equilibrium random mechanism with an enzyme-NADPH-glucose 6-phosphate dead-end complex.  相似文献   

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Sorbitol-6-phosphate dehydrogenase from loquat fruit   总被引:4,自引:3,他引:1       下载免费PDF全文
Hirai M 《Plant physiology》1979,63(4):715-717
Sorbitol-6-phosphate dehydrogenase was found in flesh tissue of mature fruit of the loquat (Eriobotrya japonica Lindl. var. Tanaka). The enzyme was purified about 30-fold from the crude extract of the fruit, and was demonstrated to catalyze sorbitol-6-phosphate + NADP glucose-6-phosphate + NADPH. The optimal pH values for sorbitol 6-phosphate oxidation and glucose 6-phosphate reduction were 9.8 and 9.1, respectively.  相似文献   

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Glucose 6-phosphate dehydrogenase (G6PD) activity was measured in individual preimplantation rabbit and mouse embryos. Substrate turnover by the enzyme is at least 30 times greater than glucose oxidation by the pentose shunt in the early rabbit embryo. There was no evidence during the preimplantation period of the embryos in either species of a bimodal distribution of G6PD activities among the embryos. Since cytological studies have not shown that inactivation of the X chromosome occurs during the early cleavage period and G6PD activity is sex-linked and gene-dose dependent in most higher animals, the evidence from the enzyme studies suggests that there is little or no synthesis of G6PD during the early preimplantation period. It is suggested that the enzyme is synthesized during oocyte development and the high levels of the enzyme found during the preimplantation period reflect the requirement of an earlier stage in oocyte development rather than the requirements of cleavage.Financial support for this work was obtained from National Institutes of Health Grants HD 03071 and HD 02315.  相似文献   

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