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  • 1
    Electronic Resource
    Electronic Resource
    ADENOSINE TRIPHOSPHATE CREATINE PHOSPHOTRANSFERASE OF RAT CEREBRAL CORTEX: EVIDENCE FOR A BIMODAL SUBCELLULAR LOCALIZATION (1968)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 15 (1968), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —(1) ATP: creatine phosphotransferase of rat cerebral cortex is soluble to the extent of 57 per cent when the tissue is homogenized in 0.25 M-sucrose and 80 per cent when distilled water is used for tissue dispersion. Among particulate fractions, the crude mitochondria] fraction contains the highest percentage of enzyme activity.(2) Discontinuous sucrose gradient fractionation of the crude mitochondrial fraction yields about 55 per cent of the particulate activity in the nerve ending fractions and 24 per cent in the mitochondrial pellet.(3) Rupturing of the nerve-ending particles by a moderate osmotic shock designed to spare the mitochondria results in about 60 per cent of the ATP:creatine phosphotransferase becoming soluble, the remainder preserving the association with heavy particles, presumably mitochondria.(4) Subfractionation of the microsomal fraction on a discontinuous sucrose gradient reveals that this particulate component of the enzyme is an adsorption artifact.(5) The overall evidence points to at least two distinct subcellular localizations of the enzyme in rat brain cortex, a major soluble component and a particulate component. It has not been unequivocally shown whether the latter, in turn, reflects the presence of a single, mitochondrial component or whether the soluble matrix of the nerve ending particles represents a third locale for the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1968.tb06182.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    PROPANEDIOL METABOLISM AND ITS RELATION TO LACTIC ACID METABOLISM (1965)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 119 (1965), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1965.tb47455.x
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  • 3
    Electronic Resource
    Electronic Resource
    Anion Inhibition of α-Glycerophosphate Dehydrogenase (1959)
    [s.l.] : Nature Publishing Group
    Nature 183 (1959), S. 889-890 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Table 1. EFFECT OF SALTS ON THE ACTIVITY OF DIALYSED X-GLYCERO- PHOSPHATE DEHYDROGENASE Salt added* Percentage inhibition None 0 Ammonium sulphate 65 Potassium sulphate 65 Sodium sulphate 67 Ammonium chloride 60 Potassium chloride 54 Sodium chloride 45 Ammonium formate 21 Ammonium ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/183889b0
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    Paper (German National Licenses)
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