• Journal of environmental and Sanitary engineering
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• v.14 no.1
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• pp.88-96
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• 1999

The effect of acute cadmium-neuropathy on phospholipid metabolism in rat sciatic nerve was investigated. An animal model of cadmium neuropathy was induced by feeding diet containing cadmium to Sprague-Dawley rat for two weeks. Four weeks aged Sprague-Dawley rats were divided into four groups : normal control group, 10ppm-cadmium treated group, 100ppm-cadmium treated group, 1000ppm-cadmium treated group, reference drug, myo-inositol-treated group. All rats were sacrificed at the end of two weeks. The rate of incorporation of 2-[3H]myo-inositol into polyphosphinositide was significantly decreased while the rates of incorporation into phospholipid of titratedserine, ethanolamine and choline were unchanged in sciatic nerve obtained from cadmium-treated rat. Continuously the activities of three enzymes concerned with inositol phospholiped metabolism were measured in homogenates of rat sciatic nerves. Cystidine diglyceride transferase and phophatidylinositol kinase showed significantly decreased activities while phosphatidylinositol-4-phosphate kinase did not show any significant change in activity by cadmium treatment. However these deficits of inositol phospholipid metabolism were ameliorated by myo-inositol administration and these effectiveness were more potent in lower dose cadmiumtreated rats than higher dose cadmium-treated rats. These results suggest that cadmium intoxicated peripheral nerve with perturbation of the ployphosphoinositide metabolism and alteration of the enzyme activity which concerned with myo-inositol metabolism.

• Bulletin of the Korean Chemical Society
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• v.27 no.3
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• pp.359-360
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• 2006

• Journal of Microbiology
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• v.42 no.1
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• pp.20-24
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• 2004

Cloned myo-inositol-1-phosphate synthase (INOS) of Drosophila melanogaster was expressed in Escherichia coli, and purified using a His-affinity column. The purified INOS required NAD$\^$+/ for the conversion of glucose-6-phosphate to inositol-1-phosphate. The optimum pH for myo-inositol-1-phosphate synthase is 7.5, and the maximum activity was measured at 40$^{\circ}C$. The molecular weight of the native enzyme, as determined by gel filtration, was approximately M$\_$r/ 271,000${\pm}$15,000. A single subunit of approximately M$\_$r/ 62,000${\pm}$5,000 was detected upon SDS-polyacrylamide gel electrophoresis. The Michaelis ($K_{m}$) and dissociation constants for glucose-6-phosphate were 3.5 and 3.7 mM, whereas for the cofactor NAD$\^$+/ these were 0.42 and 0.4 mM, respectively.

• Journal of Embryo Transfer
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• v.25 no.1
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• pp.1-7
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• 2010

The objective of this study was to examine the effect of vitamin B (pantothenic acid, folic acid, and myo-inositol) that was supplemented to embryo culture medium on in vitro development of parthenogenetically activated (PA) pig embryos. Cumulus-oocyte complexes derived from slaughtered ovaries were matured in TCM-199 supplemented with porcine follicular fluid, cysteine, pyruvate, EGF, insulin, and hormones (hCG and eCG) for the first 22 h and then further cultured in hormone-free medium for an additional 22 h. After maturation culture, metaphase II oocytes that extruded 1st polar body were electrically activated and treated with $5.0\;{\mu}g/ml$ cytochalasin B for 4 h. Then, PA embryos were cultured for 7 days in a modified NCSU-23 that was supplemented with pantothenic acid, myo-inositol, or folic acid at different concentrations ($3{\sim}300\;{\mu}M$) according to the experimental design. Myo-inositol added to culture medium did not show any beneficial or inhibitory effects on embryo cleavage and blastocyst formation. However, $300\;{\mu}M$ pantothenic acid significantly inhibited blastocyst formation compared to control (no addition) (24% vs. 36%, p<0.05). Folic acid ($300\;{\mu}M$) significantly (p<0.05) increased blastocyst formation (56%) compared to control (41%). Our results demonstrated that in vitro development of PA embryos was significantly influenced by vitamin B and addition of $300\;{\mu}M$ folic acid to culture medium improved in vitro development of pig PA embryos.

• Microbiology and Biotechnology Letters
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• v.46 no.2
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• pp.102-110
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• 2018

A bacterial strain capable of metabolizing myo-inositol (MI) and converting to other substances was isolated from soil of orchard. The isolate, named YB-46, was grown on minimal medium supplemented with MI as the sole carbon source and was presumed to belonging to genus Enterobacter according to the 16S rDNA sequence. Escherichia coli transformant converting MI into unknown metabolites was selected from a metagenomic library prepared with fosmid pCC1FOS vector. Plasmid was isolated from the transformant, and the inserted gene was partially sequenced. From the nucleotide sequence, an iolG gene was identified to encode myo-inositol dehydrogenase (IolG) consisting of 336 amino residues. The IolG showed amino acid sequence similarity of about 50% with IolG of Enterobacter aerogenes and Bacillus subtilis. The His-tagged IolG (HtIolG) fused with hexahistidine at C-terminus was produced and purified from cell extract of recombinant E. coli. The purified HtIolG showed maximal activity at $45^{\circ}C$ and pH 10.5 with the highest activity for MI and D-glucose, and more than 90% of maximal activity for D-chiro-inositol, D-mannitol and D-xylose. $K_m$ and $V_{max}$ values of the HtIolG for MI were 1.83 mM and $0.724{\mu}mol/min/mg$ under the optimal reaction condition, respectively. The activity of HtIolG was increased 1.7 folds by $Zn^{2+}$, but was significantly inhibited by $Co^{2+}$ and SDS.

• Korean Journal of Food Science and Technology
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• v.5 no.4
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• pp.240-248
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• 1973

Reduction of penta-O-acetyl-myo-inosose-2 by catalytic hydrogenation and with sodium-amalgam was carried out in alcohol solution of pH $3{\sim}4$. The former reduction product was axial-alcohol, and the latter equatorial-alcohol. On reduction of penta-O-acetyl-DL-epi-inosose-2 with sodium borohydride and sodium-amalgam in the previous condition, ax.-alcohol and eq.-alcrhol have been obtained. The synthesis of various inositol-p-hydroxybezoate are described. The esters have been characterized by paper chromatography and saponification, and their antimicrobial activities on some microbes were tested for the application of food industry. As the result, it was found that the antimicrobiol activity of epi-inositol ester was superior to its analogues.

• Journal of Microbiology and Biotechnology
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• v.13 no.6
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• pp.906-911
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• 2003

The function of genes related to spectinomycin biosynthesis (spcD, speA, speB, spcS2) from Streptomyces spectabilis ATCC 27741, a spectinomycin producer, was analyzed. Each gene was subcloned from a spectinomycin biosynthetic gene cluster and overexpressed in E. coli BL21 (DE3) using pET vector. After incubating each purified protein with its possible substrates, the final products were analyzed using high-performance liquid chromatography (HPLC). From these results, spcD, speA, and speB have been identified to be dTDP-glucose synthase, myo-inositol monophosphatase, and myo-inositol dehydrogenase, respectively. In addition, the results suggest that the spcS2 gene product functions downstream of the speB gene product in the biosynthetic pathway of spectinomycin. Taken together, the present study elucidates the early steps of the biosynthetic pathway for 6-deoxyhexose (6-DOH) part (actinospectose) and aminocyclitol part (actinamine) of spectinomycin.

• Journal of the Korean Chemical Society
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• v.26 no.1
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• pp.49-57
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• 1982

Transesterification reactions were carried out with myo-inositol and five fatty acid methyl esters such as methyl laurate, methyl myristate, methyl palmitate, methyl stearate and methyl oleate in the dimethylsulfoxide solvent. Their products were separated by both thin layer chromatography and column chromatography, and myo-inositol monoesters were quantitatively separated by counter current distribution. We measured their surface tension, foaming power and emulsifying power, determined critical micelle concentrations by the color method, and evaluated their hydrophilic-lipophilic balance. The results show that myo-inositol monoesters exhibit surface activites.

• Proceedings of the KSCN Conference
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• 1998.05a
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• pp.81-81
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• 1998

• Proceedings of KHEA Conference
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• 2005.10a
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• pp.117-117
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• 2005