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  • 1975-1979  (3)
  • 1978  (3)
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  • 1975-1979  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 30 (1978), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— A fluorometric assay for choline acetyltransferase has been developed. This assay is based on coupling the choline acetyltransferase dependent formation of acetyl-CoA from acetylcholine and coenzyme A, to the reactions catalyzed by the enzymes citrate synthase and malic dehydrogenase. Although this assay is not as sensitive as previously described radiometric assays, it can be conveniently used during enzyme purification.Employing this assay method, choline acetyltransferase has been purified from human placenta to a specific activity of 92.7 μmol acetylcholine formed/min/mg protein.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 30 (1978), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The effects of salt on the properties of human placental choline acetyltransferase have been examined. Increases in enzyme activity, thermal denaturation and susceptibility to proteolysis can be related to increases in ionic strength, rather than to specific salt effects. Increased ionic strength increases the maximal velocity (Km) of the reaction, with no change in the kinetic parameter Vmax/Km (choline). The pH-Km profile, measured over the range of 6.5–8.0, indicates the requirement of a dissociated acidic residue whose pKa is below 7.5 at high ionic strength, and a protonated residue whose pKa is above 7.5 at low ionic strength. It is proposed that the conformation of the enzyme is different at high ionic strength and at low ionic strength, and that these different conformational states of the enzyme result in different rate-determining steps of the reaction.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0002-9106
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Decidual tissue occurring within the human ovarian cortex was examined by light and electron microscopy. Of 21 ovarian specimens obtained at term (36-42 weeks of gestation), decidual cells were confirmed in each. Decidual cells were found within the tunica albuginea as single cells, in nodules, in polyps or in confluent sheets. Decidual cells exhibited several characteristics of cells engaged in secretory activity: abundant rough and smooth endoplasmic reticulum, numerous profiles of the Golgi complex and a large, euchromatic nucleus devoid of heterochromatin and displaying a prominent fibrous lamina. Peduncular protrusions at the periphery of the cell contained numerous dense bodies 0.4-0.9 μm in diameter. These dense bodies were bounded by a single membrane and contained granular subunits 30-60 nm in diameter. These granular subunits were observed in the process of apparent exocytosis, as well as free in the extracellular space. Secretory bodies and their granular content also were observed both in the region of the Golgi complex and partially extruded into peduncular processes. By far the greatest number of secretory bodies occurred within peduncular processes where they may be stored prior to release. Migration of a secretory body into a peduncular process and exocytosis from such a process appears to be an unusual mode of meocrine secretion, perhaps unique to decidual cells.
    Type of Medium: Electronic Resource
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