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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 11 (1972), S. 4415-4420 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-2761
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract. The following extracellular enzymes have been readily detected in the culture filtrates from Aeromonas salmonicida: amylase, phospholipase, lysophospholipase and ribonuclease. Amylase and phospholipase have been partially characterized. Evidence suggests that glycogen may be the natural substrate for amylase, and that the role of the enzyme in natural infection is to digest glycogen present in fish muscle. The secretion of amylase activity is suppressed by the addition of glucose to the growth medium. The amounts of amylase, phospholipase and protease that can be detected in culture filtrates decreases with increase in the growth temperature from 25 to 32°C. This marked decrease in secretion of hydrolytic enzymes occurs although the initial growth rates at 25 and 32°C are similar. Free and membrane associated ribosomes have been isolated from cultures grown at 25 and 32°C. At 32°C there is a smaller proportion of membrane-associated ribosomes and this is consistent with the hypothesis that extracellular enzymes from Aeromonas salmonicida are secreted on membrane-bound polysomes.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish diseases 13 (1990), S. 0 
    ISSN: 1365-2761
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract. The specificity of the major protease secreted by Aeromonas salmonicida has been explored using a number of proteins and p-nitroanilides as substrates. The 70kDa protease was found to hydrolyse two p-nitroanilides which have been reported to be specific substrates for thrombin. Kinetic parameters (kcat, and Km) were compared for the 70kDa protease and for thrombin as were the effects of a number of inhibitors. The 70kDa protease is able to degrade proteins which have a relatively open structure, for example, caseins or denatured bovine scrum albumin, to small fragments mostly of Mr〈2500. However, proteins with a more compact structure are more resistant to the protease. It was concluded that the 70kDa protease shows some of the specificity features of thrombin, although it is less discriminating in its choice of both low and high Mr substrates than thrombin. In preliminary experiments, the 70 kDa protease was found, like thrombin, to decrease the clotting time of rainbow trout blood. The possible physiological significance of these results is discussed.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish diseases 12 (1989), S. 0 
    ISSN: 1365-2761
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract. The proteases secreted by four strains (MT004, 1102, 480 and 480P-) of Aeromonas salmonicida grown in liquid culture have been studied. Strains MT004, 1102 and 480 all show a similar pattern with two types of proteases produced; one of molecular weight 70 000 which is active against casein and gelatin and one (or more) of lower molecular weight (about 20 000) which is (are) active against gelatin but not casein. Strain 480P- produces only the latter type of protease(s). The protease of molecular weight 70 000 is classified as a serine-type protease, but further characterization of the features of its active site has not yet proved possible. The results are discussed in terms of the previously published but often contradictory data on the proteases of A. salmonicida.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    International ophthalmology 13 (1989), S. 177-180 
    ISSN: 1573-2630
    Keywords: nocardia endophthalmitis chorioretinitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A case is presented of bilateral intraocular nocardial infection associated with lung and liver foci and responding to treatment. Difficulties in diagnosis and treatment are discussed. It is suggested that unusual infections such as this should be considered in the differential diagnosis of chorioretinitis, and should be carefully sought, especially in immunocompromised patients. However, our patient is unusual in having no evidence of immunosuppression predisposing to ocular involvement in his nocardial infection.
    Type of Medium: Electronic Resource
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