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  • Immunocytochemistry  (37)
  • mitochondria
  • Springer  (65)
  • American Chemical Society
  • American Meteorological Society
  • Nature Publishing Group
  • Springer Nature
  • 1985-1989  (63)
  • 1975-1979
  • 1970-1974  (2)
  • 1960-1964
  • 1950-1954
  • 1985  (63)
  • 1974  (2)
  • 1971
  • 1953
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  • Springer  (65)
  • American Chemical Society
  • American Meteorological Society
  • Nature Publishing Group
  • Springer Nature
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  • 1985-1989  (63)
  • 1975-1979
  • 1970-1974  (2)
  • 1960-1964
  • 1950-1954
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 1554-1557 
    ISSN: 1420-9071
    Keywords: Immunocytochemistry ; neuropeptide Y ; radioimmunoassay ; rat pancreas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Significant quantities of a newly discovered peptide, neuropeptide Y, were found in the rat pancreas, where they were localized to nerves in the exocrine parenchyma and around arterial and ductal structures. Although unaffected by surgical parasympathectomy, the periarterial and periductal nerves were abolished by chemical sympathectomy, suggesting that NPY is partially costored with sympathetic transmitters in nerve fibers.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 101-102 
    ISSN: 1420-9071
    Keywords: Rhodamine 123 ; Toxoplasma gondii ; membrane potential ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The mitochondria of living mouse fibroblasts infected withToxoplasma gondii were monitored with the cationic permeant fluorescent dye rhodamine 123. Fluorescence microscopy revealed that host cell mitochondria accumulated at the cytoplasmic surface of parasitophorous vacuoles and increased the dye uptake in the periparasitophorous vacuole asT. gondii multiplied.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 981-988 
    ISSN: 1420-9071
    Keywords: Ca, Mg, Na ; electron probe analysis ; mitochondria ; sarcoplasmic reticulum ; inositol trisphosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Electron probe microanalysis (EPMA) has been used to study the subcellular distribution of Ca, Na, K. Cl, and Mg in smooth muscle. The EPMA results indicate that the sarcoplasmic reticulum (SR) is the majorintracellular source and sink of activator Ca: norepinephrine decreases the Ca content of the junctional SR in portal vein smooth muscle. Mitochondria do not play a significant role in regulating cytoplasmic free Ca2+, but mitochondrial Ca content can be altered to a degree compatible with suggestions that fluctuations in matrix Ca contribute to the control of mitochondrial metabolism. The rise intotal cytoplasmic Ca during a maintained, maximal contraction is very much greater than the rise in free Ca2+, and is probably in excess of the known binding sites available on calmodulin and myosin. Cell Ca is not increased in normal cells that are Na-loaded. The non-Donnan distribution of Cl is not due to compartmentalization, but reflects high cytoplasmic Cl. Na-loading of smooth muscle in K-free solutions is temperature dependent, and may exhibit cellular heterogeneity undetected by conventional techniques. The total cell Mg is equivalent to approximately 12 mM, and less than 50% of it can be accounted for by binding to ATP and to actin. Mitochondrial monovalent cations in smooth muscle are relatively rapidly exchangeable.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 57-58 
    ISSN: 1420-9071
    Keywords: Drosophila melanogaster ; aldehyde dehydrogenase ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Subcellular fractionation by differential centrifugation confirms the presence of aldehyde dehydrogenase inD. melanogaster. It is found principally in the heavy mitochondrial fraction.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 484-485 
    ISSN: 1420-9071
    Keywords: Gerbil ; adrenal cortex ; isocitric dehydrogenase ; mitochondria ; steroid ; steroid hydroxylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In gerbil adrenal cortex the activity of intramitochondrial NADP-linked isocitric dehydrogenase (IDH) is up to 10-fold greater than the NAD-linked IDH. The NADP-IDH, apparent Km 0.58 mM, Vmax 280 nmoles/min/mg mitochondrial protein, appears to be the major source of reducing equivalents to support adrenal mitochondrial steroid 11B- and 19-hydroxylation in this species.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 1340-1342 
    ISSN: 1420-9071
    Keywords: Immunocytochemistry ; calmodulin ; secretory granules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Calmodulin is a regulator of several calcium-dependent cellular processes. It has been suggested that it plays a role in the mechanism of secretion. Employing an indirect immunoperoxidase technique at the light microscope level, this study demonstrates the presence of calmodulin in several exocytotic cells (mast cells, thyroid follicular cells, neurohypophyseal neurosecretory terminals, pancreaticβ-cells and pancreatic acinus cells) in rat and man. The positive staining reaction for calmodulin was granular and at least in the case of rat mast cells it appeared to be associated with the granule membrane.
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  • 7
    ISSN: 1420-9071
    Keywords: Rat liver ; cytochrome oxidase ; mitochondria ; BW755C ; 3, amino-1-[m-(trifluoromethyl)phenyl]-2-pyrazoline ; lipoxygenase inhibitor ; cyclo-oxygenase inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The interaction between BW755C (3-amino-1-[m-(trifluoromethyl)phenyl]-2-pyrazoline), a potent inhibitor of both lipoxygenase and cyclo-oxygenase, and respiratory chain in mitochondria and electron transport particles (ETP) from rat livers was examined. BW755C accelerated the oxygen uptake by mitochondria without the addition of substrate for the respiratory chain. Spectrophotometric study revealed that BW755C was quickly oxidized by cytochrome oxidase in mitochondria to a compound possessing an absorption maximum at 524 nm. p-Phenylenediamine (p-diaminobenzene, PPDA), which, like BW755C, serves as an electron donor to cytoschrome oxidase, was shown to inhibit the generation of active oxygen in macrophages; the inhibition was stronger than that of BW755C. These results strongly suggest that the oxidative conversion of BW755C by mitochondrial cytochrome oxidase is associated with its potentially inhibitory action on the active oxygen-generating system in phagocytes.
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  • 8
    ISSN: 1432-072X
    Keywords: Hansenula polymorpha ; Peroxisomes ; Methanol ; Dihydroxyacetone synthase ; Cell fractionation ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The subcellular localization of dihydroxyacetone synthase (DHAS) in the methylotrophic yeast Hansenula polymorpha was studied by various biochemical and immunocytochemical methods. After cell fractionation involving differential and sucrose gradient centrifugation of protoplast homogenates prepared from methanol-grown cells, DHAS cosedimented with the peroxisomal enzymes alcohol oxidase and catalase. Electron microscopy of this fraction showed that it contained mainly intact peroxisomes, whereas SDS-polyacrylamide gel electrophoresis revealed two major protein bands (75 and 78 kDa) which were identified as alcohol oxidase and DHAS, respectively. The localization of DHAS in peroxisomes was further established by immunocytochemistry. After immuno-gold staining carried out on ultrathin sections of methanol-grown H. polymorpha using DHAS-specific antibodies, labelling was confined to the peroxisomal matrix.
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  • 9
    ISSN: 1573-4927
    Keywords: Neurospora crassa ; cytochromes ; mitochondria ; respiration ; isoleucinevaline biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Several of the isoleucine-valine requiring mutants of Neurospora crassa have been shown to have differences in growth rate, oxygen uptake rate, cyanide sensitivity, and cytochrome spectral patterns as compared to wild type. This pleiotropic effect seems to be true for mutants with changes at all three known loci affecting isoleucine and valine biosynthesis, the iv-1, iv-2, and iv-3 loci.
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  • 10
    ISSN: 1573-4927
    Keywords: glycerol-3-phosphate dehydrogenase ; mitochondria ; mtDNA ; somatic-cell hybrids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Our previous studies using rodent/human somatic-cell hybrids suggested that the expression of human mitochondrial glycerol-3-phosphate dehydrogenase (GPDM) is dependent on the presence of human mitochondria. This has now been tested directly by analysis of GPDM activity in a series of nine hybrid-cell lines, four segregating human chromosomes and five losing rodent chromosomes (reverse segregants). The chromosome composition of the hybrids was deduced from analysis of biochemical markers and examination of G- and G11-banded metaphase spreads and the mitochondrial content was determined by Southern blot analysis, using cloned mouse and human mtDNA sequences as probes. We found that the mtDNA species present in these hybrids correlated exactly with the pattern of chromosome segregation such that the conventional hybrids contained rodent mtDNA and the reverse segregants human mtDNA. However, the pattern of GPDM expression was not directly correlated with the species of chromosomes or mitochondria present: all the hybrids showed strong rodem GPDM activity and two from each class of hybrid also showed human GPDM activity but the other hybrids were negative for human GPDM. We conclude that rodent GPDM readily integrates into human mitochondria, that the expression of rodent GPDM is not dependent on the presence of rodent mitochondria, and that GPDM is not coded by mtDNA. Human GPDM either is not capable of being inserted into the rodent mitochondrial membrane or is regulated in some way in the hybrid cells by an unidentified rodent factor.
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