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T Sugio

Publications and source records attributed to T Sugio.

At least 37 records · Page 2Linked to original sources
PubMed1999

Myotonic dystrophy associated with insulinoma.

We describe a 51-year-old man with myotonic dystrophy (MyD) associated with insulinoma. In addition to the typical symptoms of MyD, he showed hypoglycemic attacks after meals. The radiological examination and selective blood sampling revealed an insulinoma in the head of the pancreas. The tumor was resected and histopathologically diagnosed as an insulinoma. In Southern blot analysis, CTG repeat of the myotonin protein kinase gene in the insulinoma showed the longest expansion, followed by normal tissue of the pancreas, muscle and white blood cells. Therefore, microsatellite instability was the most prominent in the tumor cells.

Biomarkers, Tumor↗
PubMed1998

Purification and characterization of gallic acid decarboxylase from pantoea agglomerans T71

Oxygen-sensitive gallic acid decarboxylase from Pantoea (formerly Enterobacter) agglomerans T71 was purified from a cell extract after stabilization by reducing agents. This enzyme has a molecular mass of approximately 320 kDa and consists of six identical subunits. It is highly specific for gallic acid. Gallic acid decarboxylase is unique among similar decarboxylases in that it requires iron as a cofactor, as shown by plasma emission spectroscopy (which revealed an iron content of 0.8 mol per mol of enzyme subunit), spectrophotometric analysis (absorption shoulders at 398 and 472 nm), and inhibition of the enzyme activity by 2,2'-bipyridyl, o-phenanthroline, and EDTA. Another interesting feature of this strain is the fact that it contains a tannase, which is used together with the gallic acid decarboxylase in a two-enzyme resting cell bioconversion to synthesize valuable pyrogallol from readily available tannic acid.

Journal Article↗
PubMed1998

Isolation and some properties of cytochrome c oxidase purified from a bisulfite ion resistant Thiobacillus ferrooxidans strain, OK1-50.

Sulfite ion (HSO3-) is one of the products when elemental sulfur is oxidized by the hydrogen sulfide:ferric ion oxidoreductase of Thiobacillus ferrooxidans AP19-3. Under the conditions in which HSO3- is accumulated in the cells, the iron oxidase of this bacterium was strongly inhibited by HSO3-. Since cytochrome c oxidase is one of the most important components of the iron oxidase enzyme system in T. ferrooxidans, effects of HSO3- on cytochrome c oxidase activity were studied with the plasma membranes of HSO3(-)-resistant and -sensitive strains of T. ferrooxidans, OK1-50 and AP19-3. The enzyme activity of AP19-3 compared with OK1-50 was strongly inhibited by HSO3-. To investigate the inhibition mechanism of HSO3- in T. ferrooxidans, cytochrome c oxidases were purified from both strains to an electrophoretically homogeneous state. Cytochrome c oxidase activity of a purified OK1-50 enzyme was not inhibited by 5 mM HSO3-. In contrast, the same concentration of HSO3- inhibited the enzyme activity of AP19-3 50%, indicating that the cytochrome c oxidase of OK1-50 was more resistant to HSO3- than that of AP19-3. Cytochrome c oxidases purified from both strains were composed of three subunits. However, the molecular weight of the largest subunit differed between OK1-50 and AP19-3. Apparent molecular weights of the three subunits of cytochrome c oxidases were 53,000, 24,000, and 19,000 for strain AP19-3 and 55,000, 24,000, and 19,000 for strain OK1-50, respectively.

Drug Resistance, Microbial↗
PubMed1998

Purification and characterization of sulfur reductase from a moderately thermophilic bacterial strain, TI-1, that oxidizes iron.

A moderately thermophilic bacterium, strain TI-1, produces H2S outside of the cells when grown at 45 degrees C on Fe(2+)-medium (pH 1.8) containing elemental sulfur and L-glutamic acid. A newly identified sulfur reductase was present in the cytosol of this strain and was purified to an electrophoretically homogeneous state from strain TI-1. The apparent molecular weight of sulfur reductase was 86,000 by gel filtration and 48,000 by SDS-PAGE, so the enzyme was a homodimer. The enzyme was most active at pH 9.0 and 60 to 70 degrees C, and it catalyzed the reduction of 1 mol of elemental sulfur with 1 mol of NADH to give 1 mol of H2S and 1 mol of NAD+. Elemental sulfur was a specific electron acceptor of this enzyme. Thiosulfate, sulfite, and tetrathionate were not electron acceptors, but inhibited sulfur reductase activity. NADPH was not used as an electron donor.

Acid Phosphatase↗
PubMed1998

Fatal liver cirrhosis and esophageal variceal hemorrhage in a patient with type IIIa glycogen storage disease.

A 45-year-old woman with type IIIa glycogen storage disease (GSD IIIa) died of variceal hemorrhage secondary to liver cirrhosis. The postmortem examination disclosed increased intracellular glycogen in the liver as well as in the heart and skeletal muscle. Although most liver injuries in GSD IIIa have been considered to be non-progressive in adulthood, liver cirrhosis can be a cause of death in some patients.

Diagnosis, Differential↗
PubMed1996

[Growth hormone prevents the steroid myopathy in rats].

To clarify whether growth hormone possesses the counteracting effect on steroid myopathy, we examined the influence of simultaneous administration of recombinant human growth hormone (rhGH) with glucocorticoid on the diameter of muscle fibers in rats. Female Sprague-Dawley rats weighing 120-140 g were divided into four groups. A group treated with glucocorticoid alone was subcutaneously injected with 5 mg/kg/day triamcinolone, a GH-treated group with 10 IU/kg/day rhGH alone, a steroid-GH-group with the same doses of glucocorticoid and rhGH. The control rats were injected with the vehicle alone. After 14 days of treatment, each rat was anesthetized with ether and subjected to muscle biopsy of extensor digitorum longus (EDL) and soleus. Administration of rhGH alone failed to affect the diameter of muscle fibers in either EDL or soleus. Glucocorticoid treatment caused a significant reduction in the diameter of muscle fibers in the EDL, compared with the control. In the type II muscle fibers of the EDL, simultaneous administration of rhGH attenuated glucocorticoid-induced muscle atrophy significantly. We concluded that GH administration would at least partially prevents steroid myopathy.

Animals↗
PubMed1995

A DNA region that complements on Escherichia coli cysG mutation in Thiobacillus ferrooxidans.

Thiobacillus ferrooxidans AP19-3 has a novel NADH-dependent sulfite reductase in the periplasmic space. The gene responsible for the appearance of NADH-dependent sulfite reductase activity was cloned into a vector plasmid pBR322 to give a 5.7-kb hybrid plasmid, pTHS1, which contains a 1.3-kb DNA fragment of T. ferrooxidans AP19-3. When pTHS1 was used to transform sulfite reductase deficient E. coli mutants, strain AT2455 (cysG), JM246 (cysI), and AT2427 (cysJ), it complemented only the E. coli cysG mutation. Since cysG codes for S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase, the enzyme involved in siroheme synthesis, the results indicate that the DNA region that codes for S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase is present in a T. ferrooxidans 1.3 kb DNA fragment on pTHS1.

DNA, Bacterial↗
PubMed1994

Sensitivity of Iron-Oxidizing Bacteria, Thiobacillus ferrooxidans and Leptospirillum ferrooxidans, to Bisulfite Ion.

When grown on iron-salt medium supplemented with the bisulfite ion, Leptospirillum ferrooxidans was much more sensitive to the ion than was Thiobacillus ferrooxidans. The causes of the sensitivity of L. ferrooxidans to the bisulfite ion were studied. The bisulfite ion completely inhibited the iron-oxidizing activities of L. ferrooxidans and T. ferrooxidans at 0.02 and 0.2 mM, respectively. A trapping reagent for the bisulfite ion, formaldehyde, completely reversed the inhibition. The treatment of intact cells with 1.0 mM bisulfite ion for 1 h and washing the bisulfite ion from the cells had no harmful effects on the iron-oxidizing activity of T. ferrooxidans. However, the treatment of L. ferrooxidans with 0.1 mM bisulfite ion for 1 h completely destroyed the iron-oxidizing activity. T. ferrooxidans had sulfite:ferric ion oxidoreductase activity. In contrast, a quite low level of sulfite:ferric ion oxidoreductase activity was found in L. ferrooxidans, suggesting that it is much more difficult for L. ferrooxidans to oxidize the bisulfite ion to the less harmful sulfate than it is for T. ferrooxidans. These results suggest that the sensitivity of L. ferrooxidans to the bisulfite ion is due to a lack of an active sulfite:ferric ion oxidoreductase and the sensitivity of its iron oxidase to bisulfite ion.

Journal Article↗
PubMed1993

Isolation and characterization of a mo -reducing bacterium.

A Mo -reducing bacterium (strain 48), which grew on medium supplemented with 200 mM Mo, was isolated from stream water obtained from Chengkau, Malaysia. The chemical properties of strain 48 conform to the characteristics of Enterobacter cloacae. Under anaerobic conditions in the glucose-yeast extract medium containing phosphate ion (2.9 mM) and Mo (10 mM), the bacterium reduced Mo to form molybdenum blue. Approximately 27% of Mo added to the medium was reduced after 28 h of cultivation. The reduction of Mo with glucose as an electron donor was strongly inhibited by iodoacetic acid, sodium fluoride, and sodium cyanide, suggesting an involvement of the glycolytic pathway and electron transport in Mo reduction. NADH and N,N,N',N' -tetramethyl-p-phenylenediamine served as electron donors for Mo reduction. When NADH was used as an electron donor, at first cytochrome b in the cell extract was reduced, and then molybdenum blue was formed. Sodium cyanide strongly inhibited Mo reduction by NADH (5 mM) but not the reduction of cytochrome b in the cell extract, suggesting that the reduced component of the electron transport system after cytochrome b serves as an electron donor for Mo reduction. Both ferric and stannous ions strongly enhanced the activity of Mo reduction by NADH.

Journal Article↗
PubMed1992

Existence of a hydrogen sulfide:ferric ion oxidoreductase in iron-oxidizing bacteria.

The existence of a hydrogen sulfide:ferric ion oxidoreductase, which catalyzes the oxidation of elemental sulfur with ferric ions as an electron acceptor to produce ferrous and sulfite ions, was assayed with washed intact cells and cell extracts of various kinds of iron-oxidizing bacteria, such as Thiobacillus ferrooxidans 13598, 13661, 14119, 19859, 21834, 23270, and 33020 from the American Type Culture Collection, Leptospirillum ferrooxidans 2705 and 2391 from the Deutsche Sammlung von Mikroorganismen, L. ferrooxidans BKM-6-1339 and P3A, and moderately thermophilic iron-oxidizing bacterial strains BC1, TH3, and Alv. It was found that hydrogen sulfide:ferric ion oxidoreductase activity comparable to that of T. ferrooxidans AP19-3 was present in all iron-oxidizing bacteria tested, suggesting a wide distribution of this enzyme in iron-oxidizing bacteria.

Journal Article↗
PubMed1992

Molybdenum oxidation by Thiobacillus ferrooxidans.

Thiobacillus ferrooxidans AP19-3 oxidized molybdenum blue (Mo) enzymatically. Molybdenum oxidase in the plasma membrane of this bacterium was purified ca. 77-fold compared with molybdenum oxidase in cell extract. A purified molybdenum oxidase showed characteristic absorption maxima due to reduced-type cytochrome oxidase at 438 and 595 nm but did not show absorption peaks specific for c-type cytochrome. The optimum pH of molybdenum oxidase was 5.5. The activity of molybdenum oxidase was completely inhibited by sodium cyanide (5 mM) or carbon monoxide, and an oxidized type of cytochrome oxidase in a purified molybdenum oxidase was reduced by molybdenum blue, indicating that cytochrome oxidase in the enzyme plays a crucial role in molybdenum blue oxidation.

Journal Article↗
PubMed1992

Purification and some properties of sulfite:ferric ion oxidoreductase from Thiobacillus ferrooxidans.

Sulfite:ferric ion oxidoreductase in the plasma membrane of Thiobacillus ferrooxidans AP19-3 was purified to an electrophoretically homogeneous state. The enzyme had an apparent molecular weight of 650,000 and was composed of two subunits (M(rs), 61,000 and 59,000) as estimated by sodium sulfate-polyacrylamide gel electrophoresis. The Michaelis constants of sulfite:ferric ion oxidoreductase for Fe3+ and sulfite ions were 1.0 and 0.071 mM, respectively. Sulfite:ferric ion oxidoreductase suffered from end product inhibition by 1 mM Fe2+.

Electrophoresis↗
PubMed1990

Reduction of Cupric Ions with Elemental Sulfur by Thiobacillus ferrooxidans.

In anaerobic or aerobic conditions in the presence of 5 mM sodium cyanide, an inhibitor of iron oxidase, cupric ion (Cu) was reduced enzymatically with elemental sulfur (S) by washed intact cells of Thiobacillus ferrooxidans AP19-3 to give cuprous ion (Cu). The rate of Cu reduction was proportional to the concentrations of S and Cu added to the reaction mixture. The pH optimum for the cupric ion-reducing system was 5.0, and the activity was completely destroyed by 10-min incubation of cells at 70 degrees C. The activity of Cu reduction with S by this strain was strongly inhibited by inhibitors of hydrogen sulfide: ferric ion oxidoreductase (SFORase), such as alpha,alpha'-dipyridyl, 4,5-dihydroxy-m-benzene disulfonic acid disodium salts, and diazine dicarboxylic acid bis-(N, N-dimethylamide). A SFORase purified from this strain, which catalyzes oxidation of both hydrogen sulfide and S with Fe or Mo as an electron acceptor in the presence of glutathione, catalyzed a reduction of Cu by S, and the Michaelis constant of SFORase for Cu was 7.2 mM, indicating that a SFORase catalyzes the reduction of not only Fe and Mo but also Cu.

Journal Article↗