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PubMed1982

Possible role of oxidized glutathione for the regulation of the myocardial hexose monophosphate shunt.

Infusion of the isolated perfused Langendorff rat heart with tert-butyl hydroperoxide (3 X 10(-4) M) resulted in a marked enhancement of the concentration of oxidized glutathione, in an increase of the NADP+/NADPH ratio, and in an elevation of the available pool of 5-phosphoribosyl-1-pyrophosphate, which is one of the end products of the hexose monophosphate shunt. Since it has been shown that oxidized glutathione overcomes the inhibition of glucose-6-phosphate dehydrogenase exerted by NADPH, these results suggest that the myocardial hexose monophosphate shunt can be stimulated rapidly and markedly through this control mechanism.

Animals↗
PubMed1996

Evidence for the expression of the triosephosphate translocator gene in green and non-green tissue of tomato and potato.

Western blot analysis revealed a cross reaction of an antibody against the spinach triosephosphate translocator with 29 kDa proteins from envelope membranes of plastids from green and red tomato fruits and also of potato tuber amyloplasts. Envelope membranes from potato tubers were isolated from a homogenate of total membranes by isopycnic sucrose density gradient centrifugation. We were able to demonstrate by reverse transcription and sequencing of the PCR product that the mRNA for the triosephosphate translocator in leaves is also present in green and red tomato fruits. The mature protein consists of 330 amino acid residues and is highly homologous to the triosephosphate translocator proteins from potato and tobacco. The PCR product obtained for potato tubers was partly sequenced. It corresponds entirely to the cDNA sequence encoding the potato leaf triosephosphate translocator protein. Evidence for the expression of the triosephosphate translocator gene in various photosynthetic active and inactive tomato tissues (leaf, green fruit, red fruit, root, petal, sepal) and potato tubers was further confirmed by northern blot analysis.

Amino Acid Sequence↗
PubMed1991

Phosphoglucoisomerase-catalyzed interconversion of hexose phosphates. Study by 13C NMR of proton and deuteron exchange.

The exchange of protons and deuterons by phosphoglucoisomerase during the single passage conversion of D-[2-13C,1-2H]fructose 6-phosphate in H2O or D-[2-13C]fructose 6-phosphate in D2O to D-[2-13C]glucose 6-phosphate, as coupled with the further generation of 6-phospho-D-[2-13C]gluconate in the presence of excess glucose-6-phosphate dehydrogenase was investigated by 13C NMR spectroscopy of the latter metabolite. In H2O, the intramolecular deuteron transfer from the C1 of D-fructose 6-phosphate to the C2 of D-glucose 6-phosphate amounted to 65%, a value only slightly lower than the 72% intramolecular proton transfer in D2O. Both percentages, especially the latter one, were lower than those previously recorded during the single passage conversion of D-[1-13C,2-2H]glucose 6-phosphate in H2O or D-[1-13C]glucose 6-phosphate in D2O to D-fructose 6-phosphate and then to D-fructose 1,6-bisphosphate. These differences indicate that the sequence of interactions between the hexose esters and the binding sites of phosphoglucoisomerase is not strictly in mirror image during, respectively, the conversion of the aldose phosphate to ketose phosphate and the opposite process.

Binding Sites↗
PubMed1976

The redox state of the glutathione in the bovine corneal epithelium.

In the corneal epithelium the levels of the oxidized and reduced glutathione, the oxidized and reduced triphosphopyridine nucleotide, the glucose-6-phosphate and the 6-phosphogluconate were investigated. The in vivo steady state levels were defined by preparation procedures and by the energy state of the adenosine phosphate system. The ratios of the levels of the metabolites involved suggested that the reactions of the glucose-6-phosphate dehydrogenase and of the glutathione reductase operate dependent on the redox state of the triphosphopyridine nucleotides.

Animals↗