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  • 2000-2004  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Degradation of extracellular matrix components by defined proteinases from the greenbottle larva Lucilia sericata used for the clinical debridement of non-healing wounds (2003)
    Oxford, UK : Blackwell Science Ltd
    British journal of dermatology 148 (2003), S. 0 
    Details
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background  Larvae of the greenbottle fly Lucilia sericata are used routinely for the clinical treatment of difficult necrotic and infected wounds. Degradation by proteinases contained in larval excretory/secretory (ES) products is thought to contribute to wound debridement by removal of dead tissue. However, proteinase activity may also affect host tissue remodelling processes.Objectives  To identify proteolytic enzymes derived from L. sericata ES products with activities against fibrin and extracellular matrix (ECM) components.Methods  Larval proteinase activities were assayed in vitro using class-specific substrates and inhibitors. Their action against fibrin and ECM components was examined using sodium dodecyl sulphate–polyacrylamide gel electrophoresis.Results  Three classes of proteolytic enzyme were detected in the secretions using fluorescein isothiocyanate-labelled casein as a model substrate. The predominant activity belonged to serine proteinases (pH optima 8–9) of two different subclasses (trypsin-like and chymotrypsin-like), with a weaker aspartyl proteinase (pH 5) and a metalloproteinase (pH 9) with exopeptidase characteristics also present. Using skin-relevant ECM components as substrates L. sericata ES products solubilized fibrin clots and degraded fibronectin, laminin and acid-solubilized collagen types I and III. Hydrolysis of ECM macromolecules was inhibited by preincubating ES products with phenylmethylsulphonyl fluoride but not 4-amidinophenylmethylsulphonyl fluoride, indicating that degradation was due to the ‘chymotrypsin-like’ serine proteinase.Conclusions  These data suggest that a combination of L. sericata ES proteinases involving chymotrypsin-like and trypsin-like activities could potentially influence wound healing events when maggots are introduced into necrotic and infected wounds, with the chymotrypsin-like activity involved in the remodelling of ECM components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2133.2003.04935.x
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  • 2
    Electronic Resource
    Electronic Resource
    Study of Acetylated Food Proteins by Raman Spectroscopy (2004)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 69 (2004), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Three food proteins, soy protein isolates, spray-dried egg white, and whey protein isolates, were acetylated to varying levels, and the extent of modification was determined by wet chemistry methods. Raman spectra of the modified proteins were obtained. A new C=O stretching vibration was observed at 1737cm-1 and was attributed to ester carbonyl groups appended to the proteins during acetylation. Calibration curves were obtained by plotting the intensity ratio of this Raman band to the 1003cm-1 phenylalanine stretching band against the extent of substituted hydroxyl groups. Linear fits were obtained with correlation coefficient r〉 0.9979. The Raman spectral data were also analyzed to study the effect of acetylation on the conformation of the 3 proteins. Marked conformational changes were observed in the modified proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2004.tb13359.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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