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At least 991 records · Page 55Linked to original sources
PubMed2003

Methods used for the isolation, enumeration, characterisation and identification of Enterococcus spp. 1. Media for isolation and enumeration.

Due to their significance in food, feed, environmental and clinical samples, the detection and enumeration of enterococci have become an important issue not only in daily routine but also in current research activities. Several media and protocols have been published for diverse purposes, but there is no single method, which universally meets all requirements. Depending on the nature of the accompanying microflora and its level, certain substrates and modifications thereof have to be used, taking into account various drawbacks and advantages. In addition to the historical applications (examination of water, different kinds of foods, intestinal and other clinical specimen), the detection of vancomycin-resistant enterococci (VRE) has become an important task, since VRE have found to be frequently involved in nosocomial infections. Moreover, contradictory methodological recommendations can be found in the literature. This paper will give a systematic survey of the different media and methods proposed during the last two decades. Emphasis is placed on compositional details and on specific applications of the media described.

Animals↗
PubMed1997

Effects of eicosanoids on parameters in isolated rat hepatocytes and isolated rat hepatocyte couplets: protective effects of eicosanoid receptor antagonists.

A number of eicosanoids caused plasma membrane blebbing in hepatocytes and this could be inhibited in a dose-dependent fashion by the receptor antagonists AH6809 and ICI 192605. The pattern of effectiveness of eicosanoids interfering with canalicular vacuole accumulation in hepatocyte couplets differed from that causing blebbing; the two most effective eicosanoids here were PGD2 and PGF2 alpha.

15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5↗
PubMed1985

Isolation and characterization of heat stable proteinases from Pseudomonas isolate AFT 21.

Pseudomonas strain AFT 21 produced three heat stable extracellular proteinases in milk and nutrient broth at 7 or 21 degrees C, but the proportions depended on medium and cultivation temperature. The three proteinases were EDTA- and o-phenanthroline-sensitive metalloenzymes and were not inhibited by N-ethylmaleimide or phosphoramidon. Proteinases I and II showed maximum activity at pH 7-7.5 and proteinase III at pH 8.5. All three enzymes showed maximum activity at 45-47.5 degrees C, but had relatively high (19-27% of maximum) activity at 4 degrees C. They were unstable at 55 degrees C in phosphate buffer, pH 6.6, or synthetic milk ultrafiltrate (SMUF) containing 12 mmol Ca2+, but were stabilized by short preheating at 100 degrees C. They were extremely heat stable in both phosphate buffer and SMUF, pH 6.6, at 70-150 degrees C. Their D-values at 140 degrees C were 69, 54 and 80 s respectively. The Z-values for Pseudomonas AFT 21 proteinase III in phosphate buffer and SMUF were 29.7 and 30.3 degrees C respectively; the corresponding activation energies for inactivation were 8.7 x 10(4) J mol-1 and 9.2 X 10(4) J mol-1.

Animals↗
PubMed2000

Isolation and characterization of an avian isolate of Encephalitozoon hellem.

Members of the phylum Microspora are a group of unusual, obligate intracellular eukaryotic parasites that infect a wide range of hosts. However, there are a limited number of microsporidial infections reported in avian hosts, and no parasite species has been defined as an avian pathogen. A microsporidian organism was recovered from the droppings of a clinically normal peach-faced lovebird (Agapornis roseicollis) and established in in vitro culture. Intermittent parasite spore shedding was documented over a 2-month period using calcofluor M2R staining of cloacal swabs. The organism was identified as Encephalitozoon hellem based on protein and antigenic profiles and molecular sequencing of the small subunit and internal transcribed spacer regions of the ribosomal RNA gene.

Animals↗
PubMed1988

Isolation of multiple forms of DNA polymerase delta: evidence of proteolytic modification during isolation.

The subunit structures of a number of human placenta DNA polymerase delta preparations were investigated by Western blotting with polyclonal antisera and by activity staining following polyacrylamide gel electrophoresis. When immunoblots and activity stains were performed on different enzyme preparations, putative catalytic subunits of (a) 170, (b) 120, or (c) 50-70 kilodaltons (kDa) were observed. It was also observed that the lower molecular weight forms could be generated upon storage of the preparations. Western blotting of human placental tissue extracts showed that the major immunoreactive polypeptide was 160-170 kDa. Treatment of the extracts with trypsin or Staphylococcus aureus V8 protease led to the generation of immunoreactive polypeptides of lower molecular weights. These studies suggest that the 120-kDa and lower forms of the enzyme are generated via uncontrolled proteolysis and provide a rationale for the observation of different apparent subunit structures previously reported for DNA polymerase delta. In addition, these findings suggest that DNA polymerase delta has a catalytic domain which resides in a protease-resistant domain.

DNA Polymerase III↗
PubMed1988

Isolation and identification of seven metabolites of 25-hydroxydihydrotachysterol3 formed in the isolated perfused rat kidney: a model for the study of side-chain metabolism of vitamin D.

The in vivo metabolism of dihydrotachysterol3, an analogue of vitamin D3 and a potent calcemic factor, has been studied in the rat. This in vivo metabolism is compared to the in vitro metabolism of 25-hydroxydihydrotachysterol3 in the perfused rat kidney. Using mass spectrometry and ultraviolet spectroscopy, we have identified seven novel metabolites derived from 25-hydroxydihydrotachysterol3. The seven compounds represent intermediates on two renal pathways (24-oxidation and 26,23-lactone formation) also observed for 25-hydroxyvitamin D3. No evidence was found for the renal synthesis of a 1-hydroxylated metabolite of 25-hydroxydihydrotachysterol3 analogous to the hormone 1,25-dihydroxyvitamin D3. Two of the compounds formed in vitro, 24,25-dihydroxydihydrotachysterol3 and 25-hydroxydihydrotachysterol 26,23-lactone, were also formed in vivo. In vivo studies also revealed the formation of two other unidentified metabolites which are presumed to be formed nonrenally and may be calcemic factors. This work shows that dihydrotachysterol3 metabolism is complex and probably utilizes the same side-chain enzymes as vitamin D3. In addition, our work also confirms that intermediates postulated to lie on pathways to 26,23-lactone in the vitamin D3 series are also formed for the side chain in dihydrotachysterol3.

Animals↗