ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Three proton pumps, morphology and movements (1984)
    Springer
    Details
    Publication Date: 1984-12-01
    Print ISSN: 0145-479X
    Electronic ISSN: 1573-6881
    Topics: Biology , Chemistry and Pharmacology , Physics
    Published by Springer
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Isolation, characterization, and reconstitution of a solubilized fraction containing the hydrophobic sector of the mitochondrial proton pump (1981)
    Springer
    Details
    Publication Date: 1981-12-01
    Print ISSN: 0145-479X
    Electronic ISSN: 1573-6881
    Topics: Biology , Chemistry and Pharmacology , Physics
    Published by Springer
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    Electronic Resource
    Electronic Resource
    The mechanism of lactate transport in human erythrocytes (1978)
    Springer
    The journal of membrane biology 44 (1978), S. 25-36 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Lactate accumulates in human erythrocytes stored at 4°C in the presence of glucose. Efflux of lactate exhibits an activation energy of 22 kcal/mole and is markedly stimulated with increasing medium pH. Lactate influx into erythrocytes that were depleted of intracellular lactate by incubation at 37° at pH 8.0 was stimulated by decreasing medium pH. Under appropriate conditions the pH-dependent lactate flux was insensitive to 4-acetamido-4′-isothiocyano-2,2′-disulfonic stilbene or 4,4′-diisothiocyano-2,2′-disulfonic stilbene, inhibitors of the inorganic anion channel, while, e.g., inorganic phosphate transport was fully sensitive. These experiments as well as measurements of H+ movements associated with lactate fluxes demonstrate that lactate transport takes place via a specific monocarboxylate transporter (distinct from the inorganic ion channel) by a H+-lactate symport mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01940571
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Isolation and characterization of proteolipids from sarcoplasmic reticulum (1980)
    Springer
    The journal of membrane biology 55 (1980), S. 233-239 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary (1) A proteolipid fraction was isolated from the membranes of fragmented sarcoplasmic reticulum from rabbit skeletal muscle by extraction with acidified chloroform/methanol 2∶1. This material was further resolved on Sephadex LH-20 in acetone/methanol 2∶1. Four fractions were collected and converted into partly delipidated water-soluble form. Although the separation of the four fractions was not sharp, it was clear from SDS-urea polyacrylamide gel electrophoresis and amino acid composition that there are at least two different species of proteolipids in sarcoplasmic reticulum. (2) Some of these fractions had ionophoric activity, catalyzing the transloction of Ca2+, Mn2+, Na+ into egg phosphatidylcholine vesicles after they were incorporated into the membrane by sonication. Under these conditions cardiolipin had no ionophoric activity. (3) A Ca2+-ATPase was isolated from sarcoplasmic reticulum by the method developed for delipidation of the enzyme [Green, N.M. (1975),In: Calcium Transport in Contraction and Secretion, E. Carafoli et al., editor. pp. 339–348 North Holland, Amsterdam.] This preparation which was depleted in proteolipids, catalyzed an ATP-dependent Ca2+ transport after incorporation into phospholipid vesicles demonstrating that a single component, Ca2+-ATPase, can function in reconstituted vesicles. However, the efficiency of pumping in these vesicles was low (Ca2+/ATP〈1). We propose that the proteolipid may increase the efficiency of pumping by contributing to the formation of the transmembranous channel either by aiding in its assembly or by participating as a functional subunit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869464
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Ca2+ translocation in Ehrlich ascites tumor cells (1979)
    Springer
    The journal of membrane biology 49 (1979), S. 309-324 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Ca2+ uptake into Ehrlich ascites tumor cells was studied at 0°C in the presence of mitochondrial inhibitors, conditions that minimized complications caused by sequestration of Ca2+ into organelles or by excretion. Under these conditions Ruthenium Red inhibited Ca2+ uptake, but other previously implicated ions, such as Pi or Mg2+, had no effect. Valinomycin either inhibited or slightly stimulated Ca2+ uptake depending on the presence of excess K+ on the outside or inside of the cell, respectively. Nigericin inhibited Ca2+ transport. Based on these data we propose an electrogenic uptake of Ca2+, possibly via a Ca2+/H+ antiport mechanism. The observation that glucose inhibited Ca2+ uptake suggested that in Ehrlich ascites tumor cells an energy-driven Ca2+ expulsion mechanism is operative, similar to that in erythrocytes. Plasma membrane preparations of ascites tumor cells were found to contain a Ca2+-dependent ATPase. These preparations, when incorporated into liposomes in an inside-out orientation, catalyzed an ATP-dependent uptake of Ca2+.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868989
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Isolation, characterization, and reconstitution of a solubilized fraction containing the hydrophobic sector of the mitochondrial proton pump (1981)
    Springer
    Journal of bioenergetics and biomembranes 13 (1981), S. 375-391 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondrial ATPase ; proteolipid ; dicyclohexylcarbodiimide ; p-hydroxymercuribenzoate ; phospholipid requirements for reconstitution of ATPase ; bacteriorhodopsin ; ATP synthesis ; reconstitution of the ATPase complex ; 28,000-dalton polypeptide ; octylglucoside
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The hydrophobic sector of the mitochondrial ATPase complex was purified by sequential extraction with cholate and octylglucoside, by further differential solubilization with guanidine and cholate in the presence of phosphatidylcholine, and by fractionation with ammonium sulfate. A polypeptide with a mass of 28,000 dalton was present in the purified hydrophobic section which was cleaved by trypsin, resulting in loss of reconstitution activity. In contrast, dicyclohexylcarbodiimide-binding proteolipid remained unimpaired after exposure to trypsin. The32Pi-ATP exchange activity of the reconstituted ATPase complex was inhibited byp-hydroxymercuribenzoate, which reacted primarily with the 28,000-dalton protein, as monitored by acrylamide gel electrophoresis with14C-labeled inhibitor. The function of a 22,000-dalton polypeptide and of some minor components in the region of the proteolipid remains unknown. An examination of the phospholipid requirements for reconstitution of an active complex revealed an unexpected discrepancy. With an excess of phosphatidylethanolamine, optimal reconstitution of32Pi-ATP exchange and ATP synthesis in the presence of bacteriorhodopsin and light was achieved; at a high phosphatidylcholine:phosphatidylethanolamine ratio, the rate of ATP synthesis remained high, but the rate of32Pi-ATP exchange dropped precipitously. A new procedure is described for the reconstitution of the ATPase complex with purified phospholipids which is stable for at least 15 days.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743211
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Three proton pumps, morphology and movements (1984)
    Springer
    Journal of bioenergetics and biomembranes 16 (1984), S. 335-351 
    Details
    ISSN: 1573-6881
    Keywords: F1 ATPase ; freeze-etch electron microscopy ; proton pumps ; reconstitution ; bacteriorhodopsin ; cytochrome oxidase ; lipids of thermoacidophilic bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The diameter of F1 coupling factor and the distance it protrudes from the membrane of bovine heart submitochondrial particles were measured quantitatively using horse spleen ferritin as a standard. Employing the freeze-etch technique, particles of similar size were found on membranes of submitochondrial particles and on membranes of particles first depleted by F1, then reconstituted by addition of F1. The extramembranous size of F1 is 9.7 nm and F1 protrudes from the membrane surface by about 13.6 nm. Bacteriorhodopsin and cytochrome oxidase were incorporated into lipids derived from membranes of extremely thermoacidophilic microorganisms by the octylglucoside dilution method. The bacteriorhodopsin pump was fully functional provided high concentrations of valinomycin were added. With decanoyl-N-methylglucamide as detergent the pump was very active in the absence of valinomycin. Concentrations of gramicidin that collapsed the ΔpH in bacteriorhodopsin liposomes prepared with soybean phospholipid had little or no effect on these rigid proteoliposomes. Very high concentrations (30 µg per ml) were partially effective, suggesting a mechanism other than formation of a gramicidin dimer channel. Cytochrome oxidase lost virtually all activity when incorporated into these rigid liposomes but was fully reactivated on addition of suitable detergents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743230
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...