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Biomedical subjects

Y Takesue

Publications and source records attributed to Y Takesue.

At least 73 records · Page 4Linked to original sources
PubMed1989

Methicillin-resistant Staphylococcus aureus in nosocomial infections in the surgical ward and operating room.

In this study 214 strains of Staphylococcus aureus were isolated from clinical specimens on the surgical ward from 1983 to 1988 and in addition, 62 airborne strains were collected in the operating room. Highly methicillin-resistant strains of S.aureus (H-MRSA, MIC greater than 100 micrograms/ml) not detected in 1983 showed a significant increase in frequency by 1987 accounting for about 60% of MRSA (MIC greater than or equal to 12.5 micrograms/ml). Countermeasures instituted in 1987 such as the use of disinfectant chlorhexidine alcohol significantly decreased the frequency of MRSA and H-MRSA isolates in 1988. In our study of coagulase type, MRSA type IV strains were predominant until 1984, whereas after 1986 type II was prevalent. All airborne strains collected in the operating room were methicillin-sensitive S.aureus, with type VII currently epidemic. We therefore concluded that cross infection with MRSA took place on the surgical ward rather than in the operating room.

Cross Infection↗
PubMed1989

[Correlation between coagulase typing and antibiotic susceptibility in methicillin resistant Staphylococcus aureus].

One hundred and fifty-two strains of Staphylococcus aureus isolated from clinical specimens from 1983 to 1987 were examined in their susceptibility against various antibiotics and in their coagulase typing. The isolation frequency of methicillin resistant strains (MRSA) was 61.6%, and highly methicillin resistant (MIC greater than 100 micrograms/ml) group occupied 81.3% of MRSA in 1987. From the study of coagulase type, it was found that current epidemic strains in our ward was type II. In MRSA, type IV strains were predominantly isolated until 1984, but after 1986 most of all MRSA strains belonged to type II. According to the coagulase type-classification of MRSA, the isolation frequency of type II was 97.5% of highly methicillin resistant group. Type II strains were more sensitive to MINO and OFLX than type IV, although in the susceptibility to DMPPC type II was less sensitive than type IV. In type IV, the percentage of beta-lactamase-producing strains was 79.3%, and type II, 33.3% with the high significance of statistical difference (p less than 0.01). In conclusion, a close correlation was suggested between beta-lactamase producing activity and the mechanism of resistance to non-beta-lactam antibiotics as to MINO, OFLX in type IV strains. On the other hand, in type II strains the mechanism of resistance seemed to be simply explained by changes of penicillin-binding-protein (PBP), and there was little concern with beta-lactamase, and other antibiotic-modifying enzymes.

Anti-Bacterial Agents↗
PubMed1988

In vitro loss of hydrophobicity of trehalase from the brush border membrane of rabbit kidney cortex.

Trehalase solubilized with 0.5% Triton X-100 and 0.5% deoxycholate from the brush border membrane of rabbit kidney cortex was all adsorbed on phenyl-Sepharose equilibrated with elution buffer containing no detergents, and all the adsorbed enzyme was eluted in one peak on the addition of 0.5% Triton X-100 to the elution buffer, in contrast to the results reported by Nakano and Sacktor (J. Biochem. 97, 1329-1335 (1985], who separated two forms of trehalase differing in hydrophobicity from rabbit kidney. On concentration of detergent-solubilized extracts, followed by incubation at 37 degrees C, however, there appeared trehalase nonadsorbable on phenyl-Sepharose, i.e. a hydrophilic trehalase. Various protease inhibitors added to the concentrated extracts did not inhibit this conversion at all. The concentration-incubation treatment also increased the proportion of trehalase that interacts with Con A-Sepharose. These results indicate that kidney trehalase that interacts with Con A-Sepharose. These results indicate that kidney trehalase is susceptible to some lytic action of a factor(s) intrinsic to the brush border membrane (limited autolysis), as seen with rabbit intestinal trehalase (Yokota et al., (1986) Biochim. Biophys. Acta 881, 405-414). Therefore, in studies of the molecular form of trehalase (and other proteins) in the brush border membrane of the kidney and intestine where a lot of hydrolases exist, it is very important to take account of limited autolysis which results in some chemical modifications without affecting enzymatic activity.

Animals↗
PubMed1987

[Experimental study on the development of endotoxemia in peritonitis with special reference to route of absorption of endotoxin].

As endotoxemia develops and presents marked symptoms in severe peritonitis, the absorption route of endotoxin from the peritoneal cavity was studied in this study. Twenty-four adult mongrel dogs were divided into 4 groups as follows. Group 1: Physiological saline solution was injected intraperitoneally with thoracic duct (TD) lymph drainage. Group 2: Peritonitis was induced without lymph drainage. Group 3: Peritonitis was induced with TD lymph drainage. Group 4: Peritonitis was induced with right lymph duct (RLD) and TD lymph drainage. Peritonitis was induced by intraperitoneal injection of endotoxin (Difco 055 B5 LPS) at 0.5 mg/kg. In Group 4, the endotoxin level in lymph from RLD reached a maximum value of 4.19 X 10(7) +/- 2.32 X 10(7) pg/ml (mean +/- S.E.), while that from TD was only 7203 +/- 5022 pg/ml. The endotoxin level in the portal venous blood three hours after administration was almost within normal limits throughout the experiment. In conclusion the route of endotoxin absorption in peritonitis is considered to be via the lymphatic system and in particular RLD is assumed to play an important role.

Absorption↗
PubMed1987

[Studies on antibacterial activity of flomoxef and its distribution to serum and intraperitoneal exudate in surgery].

1. Bacteria detected in cases of acute abdominal ailments encountered in the first department of surgery at Hiroshima university and its related facilities during the recent 4 and a half years were reviewed and the antibacterial activities of flomoxef (FMOX, 6315-S) against these isolates were investigated. As a result, this antibiotic was found to show very high activities against Staphylococcus aureus, Staphylococcus epidermidis, Escherichia coli, Klebsiella pneumoniae and Proteus spp. 2. One gram of FMOX dissolved in 100 ml of physiological saline was administered by intravenous drip infusion during operation and its concentrations in serum and intraperitoneal exudate were determined. The intraperitoneal exudate concentration exceeded the serum concentration in 2 hours after the completion of the drip infusion and, reached high enough concentration to be effective against susceptible bacteria with MICs about 12.5 micrograms/ml. The above results suggested that the new cephem antibiotic FMOX for injection should be sufficiently effective against acute peritonitis.

Acute Disease↗
PubMed1986

Solubilization of trehalase from rabbit renal and intestinal brush-border membranes by a phosphatidylinositol-specific phospholipase C.

Trehalase (EC 3.2.1.28) associated with renal and intestinal brush-border membranes was solubilized by highly purified phosphatidylinositol-specific phospholipase C (EC 3.1.4.10) from Bacillus thuringiensis, but not by phosphatidylcholine-hydrolyzing phospholipase C (EC 3.1.4.3) from Clostridium welchii or phospholipase D (EC 3.1.4.4) from cabbage. The solubilized trehalase was not adsorbed on phenyl-Sepharose, indicating that it was hydrophilic. Phosphatidylinositol-specific phospholipase C also converted Triton X-100-solubilized amphipathic trehalase into a hydrophilic form. These results suggest that trehalase is bound to the membrane through a direct and specific interaction with phosphatidylinositol.

Alkaline Phosphatase↗
PubMed1986

Purification and characterization of amphiphilic trehalase from rabbit small intestine.

Rabbit intestinal trehalase (alpha,alpha-trehalose glucohydrolase, EC 3.2.1.28) was solubilized with Triton X-100 and purified in the presence of EDTA. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis in the presence of Triton X-100 or SDS. It showed amphiphilic properties on gel filtration. polyacrylamide gel electrophoresis, charge-shift electrophoresis and phenyl-Sepharose chromatography. Its molecular weight was estimated to be about 330 000 by gel filtration under nondenaturing conditions and in the presence of Triton X-100, the value being in satisfactory agreement with the sum of the weight of one Triton X-100 micelle and twice the molecular weight (105 000) of purified hydrophilic trehalase which had been deprived of the anchor segment. The two purified trehalases gave almost the same molecular weights (about 75 000) on SDS-polyacrylamide gel electrophoresis. These results suggest that intestinal trehalase consists of two subunits with a molecular weight of 75 000 and that its anchor segment is small (less than 5000). Triton X-100 extracts freshly prepared from intestinal microvilli essentially showed one form of trehalase, which behaved on phenyl-Sepharose and Con A-Sepharose chromatography in the same manner as purified amphiphilic trehalase.

Animals↗
PubMed1985

Enzyme-linked immunosorbent assay for Met-enkephalin using unconjugated enkephalin as a solid phase antigen.

This paper presents a competitive enzyme-linked immunosorbent assay for Met-enkephalin, in which there is no need for preparing any special derivative of Met-enkephalin for its optimal function as a solid-phase antigen. Immunoplate wells were first coated with free Met-enkephalin, and then incubated with antiserum and free Met-enkephalin. The antibodies bound to the solid-phase Met-enkephalin were determined by using anti-IgG conjugated to horseradish peroxidase. The detection limit of the assay was 44 fmol Met-enkephalin per well. The results also showed that Met-enkephalin bound to the solid phase can be titrated directly.

Antibody Affinity↗
PubMed1984

A two-active site one-polypeptide enzyme: the isomaltase from sea lion small intestinal brush-border membrane. Its possible phylogenetic relationship with sucrase-isomaltase.

The enzyme responsible for all of the isomaltase activity and much of the maltase activity in the small intestine of the Californian sea lion (Zalophus californianus) was isolated by detergent solubilization of the brush-border membrane, followed by immunoadsorption chromatography using antibodies directed against rabbit sucrase-isomaltase. In 0.1% Triton X-100, sea lion isomaltase occurs as a monomer of Mr = 245,000 and is composed of a single polypeptide chain. As judged from the stoichiometry of the covalent binding of the affinity label, conduritol-B-epoxide, this polypeptide chain carries two enzymatically active sites; they are apparently identical and do not show either positive or negative cooperativity. In addition to cross-reacting immunologically with rabbit sucrase-isomaltase, sea lion isomaltase has similar overall enzymatic properties, with the exception of not hydrolyzing sucrose. The Alaskan fur seal (Collarhinus ursinus) has a two-active site isomaltase; however, in contrast to the sea lion, this animal is endowed with a small but significant sucrase activity. Along with (fully active) pro-sucrase-isomaltase, sea lion isomaltase is one of the very few examples of enzymes with more than one active site on a single polypeptide chain acting "in parallel" (rather than "in series"). Furthermore, this enzyme triggers some interesting questions on the phylogenetical pedigree of small intestinal sucrase-isomaltase.

Animals↗
PubMed1984

Immunolocalization of the 33 kD protein in the microvilli of rabbit small-intestinal epithelial cells.

Rabbit small-intestinal microvilli isolated by a Ca2+ precipitation method contain a 33 kD protein, which has not been observed in microvilli isolated in the presence of Ca2+-chelators. The intracellular localization of this protein in rabbit intestinal epithelial cells was studied by immunofluorescence and immunoperoxidase microscopy, and was compared with that of aminopeptidase M, a well-known microvillus membrane-bound enzyme. The results obtained show that the 33 kD protein is located in the inside of the microvillus, but not in the terminal web of the epithelial cell. The protein may also be located on the basolateral surface of the cell.

Aminopeptidases↗
PubMed1984

Effect of TEI-4120 (3-benzoyl-N-beta-ethoxyisopropyl-2-methlindole) on carrageenan induced disseminated intravascular coagulation (DIC) in rats.

In order to evaluate TEI-4120 (3-benzoyl-N-beta-ethoxyisopropyl-2-methylindole), as a possible therapheutic compound to disseminated intravascular coagulation (DIC), DIC model in rats was induced by the treatment of lambda-carrageenan according to the method of Sugiyama et al. with minor modification. Two hours after intraperitoneal injection of lambda-carrageenan, plasma fibrinogen decreased and platelet count, prothrombin time, serial thrombin time and plasma TXB2 prolonged or increased. By use of this model, the activities of TEI-4120, new antithrombotic compound, was evaluated compared with three other compounds, aspirin, warfarin and heparin. As a result, TEI-4120 is effective in this model. Combination therapy of TEI-4120 and warfarin is more effective than single administration of TEI-4120. The effect of combination therapy of TEI-4120 and warfarin is consistent with that of heparin. The above result suggests that TEI-4120 seems to be a promising compound to the therapy of DIC.

Animals↗
PubMed1983

Effect of phloretin on Na+-dependent D-glucose uptake by intestinal brush border membrane vesicles.

In the present work we studied the effects of phloretin on Na+-dependent D-glucose uptake by brush border membrane vesicles isolated from rabbit small intestine. Phloretin had no inhibitory effect on Na+-dependent D-glucose uptake in the presence of equilibrated Na+, although it inhibited the process in the presence of a Na+ gradient. Phlorizin inhibited Na+-dependent D-glucose uptake both in the presence and in the absence of a Na+ gradient. Phloretin and phlorizin competed with each other for the inhibition of Na+-energized D-glucose uptake. These results indicate that phloretin has no direct interaction with the Na+-dependent D-glucose transporter per se, though phloretin and phlorizin may have a common step(s) in their inhibition mechanisms. Phloretin, but not phlorizin, was found to increase the equilibrium level of D-glucose uptake whether Na+ was present or not. The increase in the equilibrium level was due to phloretin-induced binding of D-glucose to the brush border membrane, but not due to an increase in the intravesicular space. It seems to occur by a mechanism different from that by which phloretin inhibits Na+-energized D-glucose uptake, because the equilibrium level of D-glucose uptake is increased by the ionized form of phloretin but Na+-energized D-glucose uptake is inhibited by the unionized form.

Animals↗
PubMed1982

A 33,000-dalton protein of the microvilli isolated from rabbit small-intestinal epithelial cells. Purification and some properties.

Actin and four major associated proteins have been identified in the microvillus cytoskeleton from chicken intestinal brush borders isolated in the presence of Ca2+-chelating agents. We have isolated microvilli from rabbit small intestine in the presence of Ca2+ and found by sodium dodecyl sulfate-gel electrophoresis that a protein of 33,000 daltons exists in a molar ratio to actin of 1:3 within the isolated microvillus. The protein could be extracted from acetone powder of microvilli in the absence, but not in the presence, of Ca2+. Thus, for its purification the acetone powder was extracted twice with buffer containing Ca2+ and then with buffer containing a Ca2+-chelator. The 33,000-dalton protein was purified from the last extract by Sephadex G-100 gel filtration and DEAE-cellulose column chromatography. The purified protein was a water-soluble monomeric protein with a molecular weight of 33,000. Antisera against the purified protein raised in guinea pigs reacted with the antigen but not with actin or tropomyosin purified from rabbit skeletal muscle. Freezing-thawing resulted in aggregation of the purified protein, and the aggregates showed filamentous and sheet-like structures. These results suggests that the 33,000-dalton protein is a major component of the microvillus cytoskeleton.

Actins↗