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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Photochemistry and Photobiology B: Biology 24 (1994), S. 187-194 
    ISSN: 1011-1344
    Keywords: Bovine retina ; Ca^2^+-ATPase ; Rod outer segment disks ; Vertebrate vision ; Visual photoreceptor
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    ISSN: 1432-072X
    Keywords: Key words K+-ATPase ; Lactobacilli ; Potassium pump ; 2 ; 3-Butanedione ; Enzyme-phosphate complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lactobacillus helveticus ATCC 15009 (wild-type) membrane preparations hydrolyzed Mg2+-ATP as a function of K+ concentration (2–200 mM). Mg2+-ATP hydrolysis by L. helveticus membranes was strongly inhibited in the absence of exogenous K+, while it amounted to 6 nmol ATP hydrolyzed min–1 (mg membrane protein)–1 at 50 mM KCl (saturating conditions) and pH 7.2. The K+-dependent ATPase of L. helveticus displayed a relatively high affinity for potassium ions (K m = 800 μM) and was not affected by pretreatment of membranes with N,N’-dicyclohexylcarbodiimide. Membrane preparations were subjected to hypotonic shock to obtain a maximum yield of open profiles. The formation of a maximum level of enzyme-phosphate complex with a molecular mass of approximately 82 kDa was induced upon treatment of L. helveticus membrane preparations with low concentrations of [γ-32P]ATP in the presence of K+ and La3+ ions and was visualized by acidic SDS-PAGE. It was concluded that L. helveticus membranes contain an inwardly directed K+ pump whose presence is discussed in terms of its putative role in cytoplasmic pH regulation.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Neurochemical research 22 (1997), S. 297-304 
    ISSN: 1573-6903
    Keywords: Ca2+-ATPase ; synaptosomes ; calcium ; neuron
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Two forms of Ca2+-pump were identified in bovine brain synaptic membranes as aspartylphosphate intermediates and were characterized. The 140 kDa and 97 kDa phosphoproteins were digested by calpain, producing two phosphorylated fragments, of M.W. 124 and 80 kDa respectively, not inhibited by thapsigargin, and displayed a trypsin digestion pattern with the formation of one phosphorylatable fragment of about 80 kDa. These results suggest that both pumps belong to the Plasma Membrane-type of Ca2+ ATPases, differing from the Sarco- or Endoplasmic Reticulum kind. A plasma membrane Ca2+-ATPase proteinaceous inhibitor with molecular weight between 6,000 and 10,000 Da was resolved from synaptic terminal cytosol, where it is enriched by fourfold with respect to frontal cortex brain cytosol. Such enrichment is already evident in the correspondent crude fractions. The presence of calcium pump and its proteinaceous inhibitor inside the synaptic terminals from bovine brain is discussed in terms of free calcium level regulation in neuron synaptoplasm.
    Type of Medium: Electronic Resource
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