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S Furuta

Publications and source records attributed to S Furuta.

At least 415 records · Page 23Linked to original sources
PubMed1982

Reflectance spectrophotometric studies on mucosal pathology of the upper airway.

Reflectance spectrophotometry analysis has been applied to the human nasal mucosa in vivo to determine the objective parameters of the colors of the mucous membrane, as well as to study the hemodynamics and enzymatic activities related to respiratory chain metabolism in the nasal mucosa. In 24 normal subjects, there were three main spectral peaks: the peak at around 500 nm (PI), the smallest at 560 nm (P2) and the highest one at 660 nm (P3). In 28 patients with nasal allergy, spectral P3 shifted remarkably toward the shorter wavelength at around 640 nm, compared to that of normal subjects. Additionally, the increment of the absorption band at P2 was also observed. These phenomena could be seen in the nasal mucosa of the subjects after use of decongestant spray. Reflectance spectrophotometric analysis will serve as a non-invasive method of giving us useful information for a further understanding of the mucosal pathophysiology of the upper airway.

Cytochrome b Group↗
PubMed1981

Age specific prevalence of anti HA in Japan--from multi-institutional analysis.

In order to estimate age specific prevalence of Anti HA in Japan, 1757 serum samples from healthy subjects or patients with nonhepatic disease taken in 6 different districts of Japan were tested for Anti HA using HAVAB Kit. Very low prevalence, less than 10%, was observed in young adults or children. These facts indicate the young Japanese are quite susceptible to HAV infection and the effective preventive measures are urgently needed. Over all prevalence of Anti HA was 56.2%. Comparing the age specific prevalence of Anti HA in Japan with those in other countries, the situation in Japan was in intermediate between highly endemic South-East region and developed European countries.

Adolescent↗
PubMed1981

Intranuclear virus-like particles in the hepatocytes of the patients with non-A, non-B hepatitis.

Liver specimens were obtained from 21 non-A, non-B hepatitis patients when their serum transaminase levels were still elevated. The specimens were investigated by transmission electron microscope in order to investigate the presence of the structure relating to this type of hepatitis. Intranuclear electron-dense aggregates of virus-like particles were observed in 2 out of 21 cases. One was an unresolved acute hepatitis case with short-incubation posttransfusion type, and the other was a chronic persistent hepatitis case without bloodtransfusion. The size of these particles varied from 22 to 28 nm in diameter. The incidence of hepatocytes with the particles was approximately 2 to 3% of the cells investigated. These particles may represent an intranuclear alteration in close association with one type of non-A, non-B hepatitis.

Adult↗
PubMed1981

alpha-Amanitin inhibits the oxidation of long chain fatty acids in mouse liver.

It was found that the injection of the extract of Amanita virosa mushroom into mice resulted in the inhibition of long chain fatty acid oxidation by liver mitochondria. The inhibition principle was identified as alpha-amanitin. The inhibition was observed several hours after the injection of alpha-amanitin at the level of about 0.2 mg/kg, which corresponded to LD50. Activities of carnitine acyltransferases, acyl-CoA dehydrogenases, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and 3-ketoacyl-CoA thiolase remained constant. Using fatty acids with various carbon chain lengths as substrates, the oxidation of long chain fatty acids was markedly inhibited with accompanying disappearance of the carnitine-dependent component. The decreases in the oxidation of medium and short chain fatty acids were less marked. It is suggested, therefore, that the site of the inhibition is the transport of long chain acylcarnitines. Peroxisomal beta-oxidation was not affected by the alpha-amanitin treatment.

Amanitins↗
PubMed1981

Properties of peroxisomal 3-ketoacyl-coA thiolase from rat liver.

Peroxisomal 3-ketoacyl-CoA thiolase has a molecular weight of 89,000 and consists of 2 polypeptide chains of identical size. The enzyme has no interchain disulfide bonds and is reversibly dissociated to an inactive monomer in the cold. Mitochondrial 3-ketoacyl-CoA thiolase and acetoacetyl-CoA specific thiolase have molecular weights of 154,000 and 149,000, respectively. They each consist of 4 polypeptide chains of identical size. Peroxisomal thiolase and mitochondrial 3-ketoacyl-CoA thiolase operate by a ping-pong mechanism. The catalytic properties, including substrate specificity, of the peroxisomal enzyme were compared to those of mitochondrial 3-ketoacyl-CoA thiolase.

Acetyl-CoA C-Acetyltransferase↗
PubMed1981

Purification and properties of rat liver acyl-CoA dehydrogenases and electron transfer flavoprotein.

Three acyl-CoA dehydrogenases and electron transfer flavoprotein, which catalyze the initial step of mitochondrial fatty acid beta-oxidation, were purified from livers of rats fed a diet containing di(2-ethylhexyl)phthalate. Three acyl-CoA dehydrogenases, classified into short chain, general, and long chain acyl-CoA dehydrogenases on the basis of their substrate specificities, each consisted of four subunits of identical size: the molecular weights of the native enzymes were 169,000 for short chain acyl-CoA dehydrogenase, 182,000 for general acyl-CoA dehydrogenase, and 168,000 for long chain acyl-CoA dehydrogenase. Electron transfer flavoprotein with a molecular weight of 57,000 consisted of heterogeneous subunits with molecular weight of 33,500 and 25,100. The catalytic properties and molecular structures of rat liver acyl-CoA dehydrogenases were similar to those of the enzymes purified from other mammalian tissues such as pig heart, pig liver, and beef kidney. We could not obtain purified preparations of the three acyl-CoA dehydrogenases from livers of the control rats although the three dehydrogenases were completely separated from each other. The enzymes from the control and the di(2-ethylhexyl)phthalate-treated rats were compared and no differences were found in molecular sizes of the native enzymes and of their subunits, substrate specificities and immunochemical reactivities.

Acyl-CoA Dehydrogenase, Long-Chain↗
PubMed1981

Induction of acyl-CoA dehydrogenases and electron transfer flavoprotein and their roles in fatty acid oxidation in rat liver mitochondria.

The capacity of mitochondrial beta-oxidation and activities of three acyl-CoA dehydrogenases and electron transfer flavoprotein in rat liver were increased after administration of peroxisome proliferators such as di(2-ethylhexyl)phthalate or p-chlorophenoxyisobutyrate. Oxygen consumption by mitochondrial beta-oxidation with palmitate, palmitoyl-CoA or palmitoylcarnitine was in the range of 0.27-0.41 mumol O2/min per g liver and the dehydrogenase activity with palmitoyl-CoA was 0.56 mumol/min per g liver. These activities were increased, after administration of peroxisome proliferators, to 0.80-1.23 mumol O2/min per g liver and 1.06-1.08 mumol/min per g liver, respectively. The time required to reach half-maximal induction of the three acyl-CoA dehydrogenases and electron transfer flavoprotein after administration of di(2-ethylhexyl)phthalate was about 5 days. On the withdrawal of the agent, the activities of these flavoproteins decreased to the control levels with half-lives of about a day.

Animals↗
PubMed1981

Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators.

The activity of long-chain acyl-CoA hydrolase in rat liver was increased by the administration of peroxisome proliferators, such as ethyl p-chlorophenoxyisobutyrate, di(2-ethylhexyl)phthalate or acetylsalicylic acid. The induced activity was mainly confined in the soluble fluid after the subcellular fractionation. The enzyme was purified nearly to homogeneity from livers of rats treated with di(2-ethylhexyl)phthalate. The specific activity of the final preparation was 247 mumol palmitoyl-CoA hydrolyzed min-1 mg protein-1. The molecular weight of the native enzyme was estimated to be 150 000 by gel filtration and that of the subunits was 41 000 by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. The activity of the enzyme was not increased but inhibited by bovine serum albumin or Triton X-100. The molecular and catalytic properties of the enzyme suggest that the induced enzyme was different from mitochondrial and microsomal long-chain acyl-CoA hydrolyses in liver.

Animals↗