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  • 1
    Electronic Resource
    Electronic Resource
    Human neutrophil phosphodiesterase (1984)
    Springer
    Inflammation 8 (1984), S. 193-199 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Extracts of human neutrophils were examined for phosphodiesterase activity using a radiochemical assay. As reported by other investigators, both high- and low-K m forms of the enzyme were found. Although calmodulin could be measured in these extracts, human neutrophil phosphodiesterase proved not to be calmodulin dependent. Activity of the neutrophil phosphodiesterase was also not altered by physiologic concentrations of indomethacin,p-bromophenacyl bromide, eicosatetraenoic acid, or eicosatetraynoic acid, all inhibitors of arachidonic acid metabolism. These results are relevant to stimulus-secretion coupling in neutrophils, wherein calmodulin-dependent reactions play a vital role.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00916094
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of a new actin-binding protein from dictyostelium discoideum (1982)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 273-285 
    Details
    ISSN: 0886-1544
    Keywords: actin gelation ; F-actin nucleation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A new actin binding protein has been purified to homogeneity from amoebae of Dictyostelium discoideum. This protein is a single polypeptide with a molecular weight of 120,000 upon sodium dodecyl sulfate gel electrophoresis. It is soluble and trypsin-sensitive, contains no carbohydrate, increases the viscosity and sedimentation rate of F actin, and inhibits the actin-stimulated Mg ATPase of rabbit muscle heavy meromyosin. The interaction of 120,000-dalton protein with F actin is not inhibited by millimolar ATP, pyrophosphate, or micromolar calcium. The 120,000-dalton actin binding protein increases the initial rate of actin polymerization and decreases the critical concentration of actin at steady state.These properties demonstrate that 120,000-dalton protein from Dictyostelium discoidum is not a myosinlike protein. Rather, this protein is probably involved in regulating the assembly of the actin cytoskeletion.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970020307
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    Paper (German National Licenses)
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