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  • Pi-ATP exchange  (2)
  • Springer  (2)
  • Elsevier
  • Oxford University Press
  • 1995-1999
  • 1980-1984  (2)
Collection
Publisher
  • Springer  (2)
  • Elsevier
  • Oxford University Press
Years
  • 1995-1999
  • 1980-1984  (2)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 14 (1982), S. 287-295 
    ISSN: 1573-6881
    Keywords: H+-ATPase ; beef heart mitochondria ; Pi-ATP exchange ; lysolecithin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The lysolecithin extraction procedure originally described by Sadleret al. (1974) has been modified to yield a H+-ATPase with high levels of Pi-ATP exchange activity (400–600 nmol × min−1 × mg−1). This activity is further enhanced (1400–1600 nmol × min−1 × mg−1) following sucrose density gradient centrifugation in the presence of asolectin. This enhancement results in part from a lipid-dependent activation and in part from removal of inactive complexes. The H+ translocating activity of the complex has been determined spectrophotometrically using binding of oxonol VI as an indicator of membrane potential. Pi-ATP exchange, ATP hydrolysis, and oxonol binding are sensitive to energy-transfer inhibitors (oligomycin, rutamycin) and/or uncouplers (DNP, FCCP).
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 16 (1984), S. 465-475 
    ISSN: 1573-6881
    Keywords: H+-ATPase ; beef heart mitochondria ; sulfhydryl groups ; maleimides ; Pi-ATP exchange ; proton translocation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Electron transport particles and purified H+-ATPase (F1-Fo) vesicles from beef heart mitochondria have been treated with two classes of thiol reagent, viz. membrane-impermeable organomercurials and a homologous series ofN-polymethylene carboxymaleimides (Mal-(CH2) x -COOH or AMx). The effect of such treatment on ATP-driven reactions (ATP-Pi exchange and proton translocation) has been examined and compared to the effects on rates of ATP hydrolysis. The organomercurials inhibited ATP-Pi exchange and one of them (p-chloromercuribenzoate) inhibited ATPase activity. Of the maleimide series (AMx), AM10 and AM11 inhibited both ATP-Pi exchange and ATP-driven membrane potential, but not ATPase activity. The other members of the series were essentially inactive.N-Ethylmaleimide was intermediate in its efficacy. Passive H+ conductance through the membrane sector Fo was 50% blocked by AM10, slightly blocked by AM2 andN-ethylmaleimide, and unaffected by the other members of the AMx series. The data imply that one -SH near the membrane surface and one -SH about 12 Å from the surface are functional in proton translocation through the H+-ATPase.
    Type of Medium: Electronic Resource
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