• The Korean Journal of Mycology
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• v.12 no.3
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• pp.111-116
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• 1984

Ribonucleic acid contents and mononucleotides distribution from the mycelium and fruit bodies of Ganoderma lucidum were studied. P.E.I. cellulose TLC and HPLC were applied in this study. The obtained results are as follows; The levels of ribonucleic acids from the young basidiocarp mycelium were higher than those of mature basidiocarp. Guanosine 5'-monophosphate and xanthosine 5'-monophosphate were found in both young basidiocarp mycelium and mature basidiocarp. The levels of guanosine 5'-monophosphate and xanthosine 5'-monophosphate from the young basidiocarp were higher than those of the mature basidiocarp. However, inosine 5'-mono­phosphate was not detected.

• Bulletin of the Korean Chemical Society
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• v.21 no.7
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• pp.709-711
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• 2000

Oxidizing metal complex mediates the electrochemical oxidation of guanine nucleotides. This catalysis results in an enhancement in cyclic voltammograms that yield the rate constant for the oxidation of guanine by the metal complex via digital simulation. The rate constant of oxidation of guanine by Ru(bpy)3(3+) is 6.4 x 10(5)M(-1)s(-l). The rate constant and the enhanced current depend on the number of phosphate groups on the sugar of nucleotidc. Also the modified guanine bases show different oxidation rate constants following the trend guanine-5'- monophosphatc (GMP) > 8-bromo-guanine-5'-monophosphate (8-Br-GMP) > xanthosine -5'-monophosphate (XMP) > inosinc-5'-monophosphate (IMP). The guanine bases derivatized differently are all distinguishable from one another, providing a basis for studying electrochemistry of DNA and RNA and developing electrochemical biosensors.

• BMB Reports
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• v.35 no.4
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• pp.403-408
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• 2002

A hypothetical 21.0 kDa protein (ORF O197) from Escherichia coli K-12 was cloned, purified, and characterized. The protein sequence of ORF O197(termed EcO197) shares a 33.5% identity with that of a novel NTPase from Methanococcus jannaschii. The EcO197 protein was purified using Ni-NTA affinity chromatography, protease digestion, and gel filtration column. It hydrolyzed nucleoside triphosphates with an O6 atom-containing purine base to nucleoside monophosphate and pyrophosphate. The EcO197 protein had a strong preference for deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP), while it had little activity in the standard nucleoside triphosphates (dATP, dCTP, dGTP, and dTTP). These aberrant nucleotides can be produced by oxidative deamination from purine nucleotides in cells; they are potentially mutagenic. The mutation protection mechanisms are caused by the incorporation into DNA of unwelcome nucleotides that are formed spontaneously. The EcO197 protein may function to eliminate specifically damaged purine nucleotide that contains the 6-keto group. This protein appears to be the first eubacterial dITP-and XTP-hydrolyzing enzyme that has been identified.

• Korean Journal of Food Science and Technology
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• v.13 no.2
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• pp.121-126
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• 1981

An adenine-guanine doubless and $\beta$-alanine requiring mutant, D-1550-40, which had been derived from Brevibacterium ammoniagenes ATCC 6872, produced a copious amount of xanthosine-5'-monophosphate (XMP). The optimum concentration of adenine and guanine for maximal accumulation of XMP was about 75 ml/l and 100 ml/l for growth. Concentrations higher than 100 mg/l of adenine and guanine inhibited cell growth and XMP accumulation strongly. The inhibition, however, could be recovered by adding $100{\mu}g$ of biotin per liter or 0.3% of casamino acids to the culture solution. High concentrations of phosphate and magnesium salts (1.0 to 1.5%(w/v) in media) were found to be indispensable for XMP accumulation, and the presence of manganese in the culture medium stimulated both growth of cells and accumulation of XMP leaving 5'-inosinic acid unaffected. The maximal accumulation of XMP reached to 60.5 mg/l after 4 days of fermentation which had been started with a medium containing 100 mg of adenine-guanine, 5 mg of $MnSO_4{\cdot}H_2O$ and $100{\mu}g$ of biotin per liter. The specific XMP synthesis(mg of XMP/mg of cells) was increased with the increase of the cell growth rate.

• Analytical Science and Technology
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• v.23 no.6
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• pp.531-536
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• 2010

A quantitative analytical method has been established for the measurement of inosine 5'-monophosphate dehydrogenase (IMPDH) activity in human peripheral blood mononuclear cells (PBMCs) by ion-pair reversed-phase high performance liquid chromatography equipped with ultraviolet detection (HPLC/UV). IMPDH is a ${\beta}$-nicotinamide adenine dinucleotide hydrate (NAD+)-dependent dehydrogenase in which the enzyme converts inosine 5'-monophosphate (IMP) into xanthosine 5'-monophosphate (XMP). Its activity was measured by quantifying a HPLC chromatogram corresponding to XMP produced during the incubation of lysed PBMCs with IMP as a substrate and $NAD^+$ as a coenzyme. XMP produced was detected at a wavelength of 260 nm. The mobile phase was composed of a mixture of 37 mM potassium dihydrogen phosphate containing 7 mM tetra-n-butylammonium hydrogen sulfate adjusted to pH 5.5 and methanol (85:15, v/v) with a flow rate of 1 mL/min. The calibration curve was linear ($r^2$=0.999999) in the range of $0.2-50.0\;{\mu}M$ and the limit of quantification (LOQ) was $0.2\;{\mu}M$. The intra- and inter-day precisions were between 0.88-1.47% and 0.85-5.24%, respectively. The intra- and inter-day accuracies were between 98.74-99.99% and 99.95-101.65%, respectively. IMPDH activity in 11 Korean healthy volunteers ranged from 18.29 to 36.60 nmol/h/mg protein (mean = $27.70{\pm}6.28\;nmol/h/mg$ protein).

• Korean Journal of Microbiology
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• v.47 no.3
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• pp.249-254
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• 2011

Mycophenolic acid blocking the synthesis of xanthosine monophosphate is a nonnucleoside inhibitor of inosine monophosphate dehydrogenase. Therefore mycopholoic acid is a drug currently used as immunosuppressive agent in transplantation of heart, kidney and liver. Mycophenolic acid has been industrially produced through fermentation process by fungus Penicillium brevi-compactum. In this study, the profile of mycophenolic acid fermentation was observed in 5L-jar fermentor to investigate the utilization of carbon and nitrogen sources and the production of mycophenolic acid. It was investigated that what kind of carbon sources was better to cell growth and mycophenolic acid production. Fructose was the best carbon source for mycophenolic acid fermentation, but it is the most expensive one. Thereafter molasses containing sucrose as the supply source of fructose was confirmed to be the best carbon source for the industrial production. Use of molasses increased the fermentation yield of mycophenolic acid more than two times higher than glucose. It was confirmed that urea was the best inorganic nitrogen source, which did not give rise to sudden drop of culture pH. Addition of urea increased the fermentation yield of mycophenolic acid about 3.6 times higher than addition of ammonium nitrate as control. Casein, peptone and casamino acid originated from milk protein increased the fermentation yield of mycophenolic acid about 3.4 times higher than control. Peptone and casamino acid, which are casein hydrolysates, increased cell growth considerably as well.