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  • 1970-1974  (5)
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 3574-3578 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 93 (1973), S. 65-85 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In the present work the chemical cell wall composition and some other biochemical characteristics were studied in staphylococci with the intention of utilizing the data obtained in their classification. According to the cell wall peptidoglycans and teichoic acids, the 130 strains of staphylococci studied are divided into 10 major groups. This division of staphylococci into groups is in good agreement with their present classification only in some cases. All of the 47Staphylococcus aureus strains contain a cell wall peptidoglycan of thel-Lys-Gly5–6 type and ribitol teichoic acid. Coagulase-negative staphylococci are more heterogeneous and are divided according to their cell wall composition into 9 major groups. 21 strains of them are classified asS. epidermidis sensu stricto. They form a natural group and are distinguished by the occurrence of thel-Lys-Gly4–5,l-Ser0.5–1.8 peptidoglycan type, glycerol teichoic acid and anl-lactate dehydrogenase which is activated by fructose-1,6-diphosphate. 8 strains with peptidoglycan of thel-Lys-Gly4–5,l-Ser0.5–1.8 type and ribitol teichoic acid are labeled asS. saprophyticus. The remaining groups have not been given species names and require further extensive comparative study.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 93 (1973), S. 245-258 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Determination of the primary structure of the peptidoglycan of 8 strains of Peptococcus showed that 4 different peptidoglycan types occur. P. prevotii ATCC 9321 and P. grigoroffii H40/10 contain the l-Lys-d-Glu type with glycine in position 1 of the peptide subunit. P. variabilis ATCC 14955 and H 39/5, P. activus H22/12 and P. anaerobius H/7 show the l-Lys-Gly type with glycine in position 1 of the peptide subunit. P. aerogenes ATCC 14963 contains the l-Orn-d-Glu type and P. saccharolyticus ATCC 14953 the l-Lys-Gly4, l-Ser1type. The occurrence of these different peptidoglycan types is a valuable criterion for the classification of peptococci. The following conclusions were made: P. saccharolyticus had to be excluded from Peptococcus. P. variabilis and P. anaerobius can be united within one species, whereas P. prevotii ATCC 9321 and P. aerogenes ATCC 14963 can not be included in one species as has been suggested before. P. grigoroffii H40/10 and P. activus H22/12 were wrongly classified.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 71 (1970), S. 271-282 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung Die quantitative Aminosäurezusammensetzung des Mureins von M. flavum, M. thermosphactum, M. lacticum und M. liquefaciens wurder untersucht. Das Murein von M. flavum und M. thermosphactum weist folgende Molverhältnisse auf (auf- bzw. abgerundete Zahlen): DAP:Glu:Ala=1:1:1,5-1,7. Außerdem konnten 1,8 Mol Ammoniak pro Mol Glutaminsäure gefunden werden, was für ein Vorliegen von Glu und DAP als Amid spricht. Für das Murein von M. lacticum und M. liquifaciens ergeben sich folgende auf- bzw. abgerundete Molverhältnisse: M. lacticum: Hyg + Glu:Gly:L-Lys:D-Ala=1:2:2:1; M. liquefaciens: Hyg + Glu:Gly:hsr:D-Orn:D-Ala=1:2:1:1:1. Die Aminosäuresequenz des Mureins von M. liquefaciens konnte durch die Analyse der in den sauren Partialhydrolysaten der Zellwände auftretenden Peptide bestimmt werden. Das Murein von M. liquefaciens weist eine ähnliche Aminosäuresequenz wie das Murein von M. lacticum auf. Das an die Muraminsäure gebundene Tetrapeptid zeigt die Sequenz: Gly-Hyg(Glu)-Hsr-D-Ala. Die an der Quervernetzung beteiligte Interpeptidbrücke Nδ-Gly-D-Orn ist mit seinem Glycinende an die α-Carboxylgruppe der Hyg (Glu) und mit der α-Aminogruppe des D-Orn an das D-Ala einer benachbarten Peptiduntereinheit gebunden. Die Primärstruktur des Mureins von M. flavum und M. thermosphactum dagegen gleicht der des Mureins von Corynebacterium diphtheriae, wie aufgrund der quantitativen Aminosäurezusammensetzung und der „Fingerprints” von Partialhydrolysaten gefolgert werden konnte. M. flavum und M. thermosphactum unterscheiden sich aber nicht nur in ihrem Mureinaufbau, sondern auch in ihrer Morphologie und bestimmten physiologischen Merkmalen von M. lacticum und M. liquefaciens. Sie gleichen mehr den menschen- und tierpathogenen Corynebakterien und sollen daher aus der Gattung Microbacterium eliminiert werden. M. lacticum und M. liquefaciens zeigen dagegen eine weitgehende Ähnlichkeit mit bestimmten pflanzenpathogenen Corynebakterien.
    Notes: Summary The quantitative amino acid composition of the murein of M. flavum, M. thermosphactum, M. lacticum and M. liquefaciens was determined. The murein of M. flavum and M. thermosphactum contains DAP, Blu and Ala at a molar ratio of about 1:1:1,5-1,7. In addition, 1,8 moles of ammonia were found per mole of glutamic acid, indicating, that both DAP and Glu are present as amides. The murein of M. lacticum and M. liquefaciens showed the following molar ratios. M. lacticum: Hyg1+Glu:Gly:L-Lys:D-Ala=1:2:2:1; M. liquefaciens: Hyg+Glu:Gly:Hsr: D-Orn:D-Ala=1:2:1:1:1. The amino acid sequence of the murein of M. liquefaciens was determined by analysing the various peptides from acid partial hydrolysates of the cell walls. The murein of M. liquefaciens resembles the murein of M. lacticum. The tetrapeptide bound to the muramic acid has the sequence: Gly-Hyg(Glu)-Hsr-D-Ala. The cross-linkage is performed in the same way as in M. lacticum. The interpeptide bridge Nδ-Gly-D-Orn is bound by its glycine end to the α-carboxyl group of Hyg(Glu) and by the α-amino group of D-Orn to D-Ala of an adjacent peptide subunit. The primary structure of the murein of M. flavum and M. thermosphactum is similar to that of the murein of Corynebacterium diphtheriae as has been shown by the quantitative amino acid composition and the fingerprints of the partial hydrolysates of the cell walls. M. flavum and M. thermosphactum can be distinguished from M. lacticum and M. liquefaciens not only by murein type but also in morphology and certain physiological characteristics. They are closely related to the human and animal pathogenic corynebacteria and should be removed from the genus Microbacterium. M. lacticum and M. liquefaciens, on the other hand, differ significantly from human and animal pathogenic corynebacteria and show greatest similarity to certain plant pathogenic corynebacteria.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1440
    Keywords: Shock ; endotoxin ; mucopeptide ; limulus-test ; Schock ; Endotoxin ; Mucopeptid ; Limulus-Test
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Nicht nur die Endotoxine gramnegativer Bakterien, sondern auch die Mucopeptide verschiedener grampositiver Erreger können eine Gelierung von Amöbocytenlysaten ausLimulus polyphemus (LPL) hervorrufen. Offenbar abhängig von dem Grad der Solubilisierung ist die Wirksamkeit der Mucopeptide zwischen 1000 und 100000mal geringer als die von Endotoxin. Im Gegensatz zu Endotoxin hat die Behandlung von Mucopeptid mit Lysozym eine Abnahme bzw. einen vollständigen Verlust seiner Aktivität im LPL-Test zur Folge. Ein so behandeltes Mucopeptid ist im einfachen Capillarpräcipitationstest unter Verwendung von Antiseren gegen Mucopeptid ebenfalls nicht mehr präcipitierbar. Die Möglichkeit, die LPL-Aktivität von Mucopeptid durch Vorbehandlung mit Lysozym aufzuheben, erlaubt eine Abgrenzung gegenüber der Endotoxin-bedingten LPL-Gelierung. Bei im LPL-Test positiven Blutproben von Patienten mit Verdacht auf Endotoxämie könnte also eine Mucopeptid-induzierte LPL-Reaktion durch Vorbehandlung mit Lysozym ausgeschlossen werden.
    Notes: Summary Gelation of amebocyte lysate fromLimulus polyphemus (LPL) is induced not only by endotoxins of gramnegative bacteria but also by mucopeptides of various grampositive organisms. Solubilization considerably increases mucopeptide LPL-activity. Total activity of mucopeptide, however, is about 1000-100 000 times smaller than that of endotoxin. In contrast to endotoxin, treatment of mucopeptide with lysozyme causes decrease or complete loss of LPL-activity. Also mucopeptide thus handled does not react any more in the capillary precipitin test. The possibility to destroy mucopeptide LPL-activity by pretreatment with lysozyme permits differentiation from LPL-gelation by endotoxin. In blood specimens of patients with suspected endotoxemia and positive LPL-test mucopeptide induced LPL-reaction therefore can be excluded by pretreatment with lysozyme.
    Type of Medium: Electronic Resource
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