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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 763 (1995), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The fumarate reductase operon of Wolinella succinogenes is made up of three structural genes (frd-CAB). The frdC gene was located next to the promoter region and identified as the cytochrome b structural gene encoding 256 amino acid residues. The N-terminal amino acid sequences of seven fragments derived from the cytochrome b moiety of the enzyme all mapped within the frdC gene. This suggested that the enzyme contained only one species of cytochrome b. Re-evaluation of earlier measurements of subunit composition, haem B content and molecular weight led to the conclusion that the enzyme contained one molecule of cytochrome b with two haem B groups. The hydropathy plot of the amino acid sequence predicted five membrane-spanning hydrophobic segments, the first four of which contained a single histidine residue each. These residues could form the axial ligands to the two haem B groups. FrdC was found to be homologous with the cytochrome b (SdhC) of the Bacillus subtilis succinate dehydrogenase, but not with the hydrophobic subunits of the fumarate reductase or succinate dehydrogenase of Escherichia coli.
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Social Science & Medicine 34 (1992), S. 625-637 
    ISSN: 0277-9536
    Keywords: Colombia ; anthropology ; malaria ; self-diagnosis ; self-treatment
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Social Science & Medicine 17 (1983), S. 147-161 
    ISSN: 0277-9536
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Social Science and Medicine. Part B Medical Anthropology 15 (1981), S. 535-539 
    ISSN: 0160-7987
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 212 (1966), S. 301-302 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Leptotrichia buccalis endotoxin and a repurified, commercially available endotoxin of Escherichia coli 0111 : .B4 (Difco Laboratories) were analysed for phosphorus5, total reducing sugars6, hexosamine7 and nitrogen8. L. buccalis endotoxin contained 1-0 per cent nitrogen, 0-9 per cent phosphorus, 60 ...
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 48 (1970), S. 723-728 
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary The capillary blood flow in the pancreas and mesenteric fatty tissue of rabbits was observed by means of a pancreas chamber technique. The influence of intravenously infused cottonseedoil emulsions (Lipofundin®) on the corpuscular blood flow in capillaries was measured. The corpuscular velocity was decreased in every case of oil injection but no change could be registered after the infusion of the pure emulsifying agent. The most important parameters of the flow (arterial and venous blood pressure, body and object temperature, hematocrit and heart rate) were found to be constant during the time of observation. Only a short and low decrease of the heart frequency was recorded after the maximal fat intake (2 g fat/kg body weight). Big changes of the hematocrit had a significant influence on the corpuscular flow velocity. During hyperlipemia the capillary bed was overcrowded of fat droplets. The intensity and frequency of the rhythmically alternating capillary flow was changed. The resting of erythrocytes in some capillaries during the whole hyperlipemic phase or flow phenomena during the decrease and increase of the microcirculatory flow velocity are discussed under the viewpoint of fluid mechanics. There was a correlation between the corpuscular flow velocity and the thickness of the marginal plasma layer. The decrease of corpuscular velocity after fat injection was larger in capillaries with a big plasma zone than in capillaries with a small one. This „inversion phenomenon“ is interpretated rheologically and its possible physiological importance is pointed out.
    Notes: Zusammenfassung Die Capillarströmung im Pankreas und Mesenterialfettgewebe wurde bei Kaninchen vitalmikroskopisch untersucht. Gemessen wurde der Einfluß von parenteral zugeführter Baumwollsaatöl-Emulsion (Lipofundin®) auf die intracapilläre Corpuscularströmungsgeschwindigkeit. Stets kam es zu einer deutlichen Strömungsverlangsamung, die nach Infusion mit ölfreier Emulgatorlösung ausblieb. Die wichtigsten Strömungsparameter (zentraler Arterienund Venendruck, Körperkern- und Objekttemperatur, Hämatokrit und Herzfrequenz) wurden während der Versuchsdauer — außer bei maximaler Fettbelastung (2 g Fett/kg KG) — konstant gefunden. Starke Schwankungen des Hämatokrit hatten einen statistisch signifikanten Einfluß auf die corpusculäre Strömungsgeschwindigkeit. Während der zweistündigen Lipämiephase war das Capillarbett von 1–2 µ großen Fettröpfchen überschwemmt. In diesem Zeitraum ließen sich Veränderungen in der Rhythmik der Durchströmung sowie völlige Strömungsruhe in manchen Capillaren nachweisen. Diese Phänomene werden nach flüssigkeitsmechanischen Gesichtspunkten interpretiert. Eine Korrelation zwischen der Corpuscularströmungsgeschwindigkeit und der Dicke des Plasmarandsaumes konnte nachgewiesen werden. In Capillaren mit weitem Plasmarandsaum wurde die Durchströmung stärker durch die eingeschwemmten Fettpartikel alteriert als in solchen ohne randständige Plasmazone. Dieses „Inversionsphänomen“ wird rheologisch gedeutet und auf seine physiologische Bedeutung hin untersucht.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 163 (1995), S. 432-438 
    ISSN: 1432-072X
    Keywords: Key words Quinol oxidase ; Bacillus subtilis ; Electron ; transport ; Respiration ; Menaquinone ; qox Deletion ; mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Menaquinol oxidase isolated from the membrane of Bacillus subtilis W23 was found to consist of four polypeptides (QoxA, B, C, and D) that were predicted by the sequence of the qox operon of B. subtilis 168 (Santana et al. 1992). The preparation contained 7 mol cytochrome aa 3 per g protein, which corresponds to 2 mol heme A per mol enzyme of 144 kDa molecular mass. Respiration with dimethylnaphthoquinol catalyzed by the enzyme was ten times faster than that with menadiol. Activities with more electropositive quinols were negligible. The activity of the enzyme was inhibited by equimolar amounts of HQNO, while antimycin, myxothiazol, and stigmatellin were more than tenfold less effective. When cells of both strains of B. subtilis (W23 and 168) were grown with glucose, quinol respiration was an order of magnitude more active than respiration with N,N,N',N'-tetramethyl-1,4-phenylenediamine plus ascorbate. Surprisingly, the same result was obtained with mutant strains lacking qoxB. As cytochromes a and d were virtually absent, a second quinol oxidase, possibly of the cytochrome o-type, was apparently formed by the mutants.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 149 (1988), S. 572-579 
    ISSN: 1432-072X
    Keywords: Sulphur reductase ; Sulphur respiration ; Electron transport ; Reconstitution ; Wolinella succinogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wolinella succinogenes can grow at the expense of sulphur reduction by formate. The enzymes involved in the catalysis of this catabolic reaction have been investigated. From the results the following conclusions are drawn: 1. The enzyme isolated as a sulphide dehydrogenase from the cytoplasmic membrane of W. succinogenes is the functional sulphur reductase that operates in the electron transport from formate to sulphur. 2. The enzyme (Mr 200,000) consists essentially of one type of subunit with the Mr 85,000 and contains equal amounts of free iron and sulphide (120 μmol/g protein), but no heme. It represents the first functional sulphur reductase ever isolated. 3. The electron transport chain catalyzing sulphur reduction by formate consists merely of formate dehydrogenase and sulphur reductase. A lipophilic quinone which mediates the transfer of electrons between enzymes in other chains, is apparently not involved. This is the first known example of a phosphorylative electron transport chain that operates without a quinone. 4. The same formate dehydrogenase appears to operate in the electron transport both with sulphur and with fumarate as the terminal electron acceptor in W. succinogenes.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-072X
    Keywords: Formate dehydrogenase ; Wolinella succinogenes ; Molybdoenzymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The formate dehydrogenase of Wolinella succinogenes is a membraneous molybdo-enzyme which is involved in phosphorylative electron transport. The gene (fdhA) encoding the largest subunit was isolated from a gene bank by immunological screening. The fdhA gene was located in an apparent transcriptional unit (fdh A, B, C. D) together with three more structural genes. The N-terminal sequences of three polypeptides present in the isolated enzyme were found to map within the fdhA, B and C structural genes. A polypeptide corresponding to fdhD was not detected in the enzyme preparation. This suggested that the functional formate dehydrogenase was made up of three or four different subunits. The genes fdhA and C encode larger preproteins which differ from the corresponding mature proteins by N-terminal signal peptides. The N-terminal half of the mature FdhA is homologous to the larger subunits of the formate dehydrogenases of E. coli (formate-hydrogenlyase linked) and Methanobacterium formicicum as well as to three bacterial reductases containing molybdenum. It harbours a conserved cysteine cluster and two more domains which may be involved in binding the molybdenum cofactor. FdhB may represent an iron-sulphur protein, twelve cysteine residues of which are arranged in two clusters which are typical of ligands of the iron-sulfur centers in ferredoxins. FdhC is a hydrophobic protein with four predicted transmembrane segments, which appears to be identical with the cytochrome b present in the isolated formate dehydrogenase. It may form the membrane anchor of the enzyme and react with the bacterial menaquinone.
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