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  • Chitin synthetase  (3)
  • Springer  (3)
  • Periodicals Archive Online (PAO)
  • Wiley-Blackwell
  • 1985-1989  (3)
  • 1987  (3)
Collection
Keywords
Publisher
  • Springer  (3)
  • Periodicals Archive Online (PAO)
  • Wiley-Blackwell
Years
  • 1985-1989  (3)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Stabilization of chitin synthetase and purification of chitosomes from several mycelial Mucorales (1987)
    Springer
    Antonie van Leeuwenhoek 53 (1987), S. 171-181 
    Details
    ISSN: 1572-9699
    Keywords: Chitin synthetase ; chitosomes ; Mucorales
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Stability of chitin synthetase in cell-free extracts from mycelial fungi was markedly improved by the presence of sucrose in the homogenization media. Breakage of mycelium in sucrose-containing buffer yielded enzyme preparations from which chitosomal chitin synthetase could be purified by a procedure involving ammonium sulfate precipitation, gel filtration and centrifugation in sucrose density gradients. Purified chitosomes catalyzed the synthesis of chitin microfibrils in vitro upon incubation with substrate and activators. Chitosomal chitin synthetase from the filamentous form of M. rouxii was similar to the enzyme from yeast cells, except for the poorer stability and diminished sensitivity to GlcNAc activation of the former.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00393845
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  • 2
    Electronic Resource
    Electronic Resource
    Activation of chitin synthetase from Phycomyces blakesleeanus by calcium and calmodulin (1987)
    Springer
    Archives of microbiology 148 (1987), S. 280-285 
    Details
    ISSN: 1432-072X
    Keywords: Chitin synthetase ; Phycomyces blakesleeanus ; Calcium-calmodulin ; Proteases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Levels of basal chitin synthetase in cell-free extracts from Phycomyces blakesleeanus were reduced by breakage of cells in the presence of EDTA or EGTA. Addition of Ca2+ to these extracts activated chitin synthetase. Maximal activation was obtained after 2 h at a Ca2+ concentration of 2–5 mM. Activation by calcium was not reduced by any protease inhibitor tested but benzamidine, whereas the weak proteolytic activity of the extracts was inhibited by antipain. Larger levels of chitin synthetase activation were obtained by the simultaneous addition of calcium and calmodulin in most, but not all extracts. This further activation by calmodulin was prevented by TFP. ATP or cAMP did not stimulate activation by calcium or calcium-calmodulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00456705
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  • 3
    Electronic Resource
    Electronic Resource
    Separation of chitosomes and secretory vesicles from the “slime” variant of Neurospora crassa (1987)
    Springer
    Archives of microbiology 149 (1987), S. 156-162 
    Details
    ISSN: 1432-072X
    Keywords: “Slime” variant ; Neurospora ; Chitosomes ; Chitin synthetase ; Secretory vesicles ; Invertase ; Phosphatase ; Membranes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cells from the “slime” variant of Neurospora crassa were broken in isotonic conditions by use of triethanolamine buffer plus EDTA. After removal of large membranous structures by low-speed centrifugation, chitosomes and secretory vesicles were separated by means of gel filtration, precipitation of membranous contaminants with Concanavalin A, and centrifugation in sucrose or glycerol gradients. Polypeptidic composition of fractions enriched in secretory vesicles or chitosomes was found to be distinct. By these criteria we concluded that chitosomes and secretory vesicles represent different populations of microvesicles. Both microvesicular populations appeared free of endoplasmic reticulum and vacuolar contaminants as demonstrated by determination of appropriate enzymatic markers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425082
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