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  • 1
    Electronic Resource
    Electronic Resource
    Extracellular, Extravascular Carbonic Anhydrase in Skeletal Muscle (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 429 (1984), 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.1749-6632.1984.tb12367.x
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  • 2
    Electronic Resource
    Electronic Resource
    Carbonic Anhydrase in Human Platelets: Effects of Carbonic Anhydrase Inhibition on Platelet Aggregation (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 429 (1984), 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.1749-6632.1984.tb12334.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Membrane-associated carbonic anhydrase IV in skeletal muscle: subcellular localization (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 405-411 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Carbonic anhydrase IV (CA IV) was examined by light microscopy and electron microscopy in rat soleus muscle. Semithin sections of aldehyde-fixed Epon-embedded muscle were stained with rabbit anti-rat lung CA IV and the avidin-biotin-peroxidase complex. With this technique, capillaries and sarcolemma showed positive CA IV staining. For electron microscopy, rat soleus specimens were aldehyde-fixed, with or without subsequent osmication, and embedded in Epon. Ultrathin sections were immunostained with anti-rat lung CA IV/immunogold. Omitting osmium allowed ample antigen-antibody reactions but could not prevent the release of glycosylphosphatidylinositol-anchored CA IV from the membranes, which led to apparent background staining. Postosmication significantly reduced tissue antigenicity but kept the antigen bound to the membranes and thus allowed a very precise localization of CA IV. By electron microscopy, membrane-bound CA IV is found to be associated with capillary endothelium, sarcolemma, and sarcoplasmic reticulum (SR). Conceivably, the presence of SR staining in ultrathin sections and its absence in semithin sections reflect a problem of accessibility of the antigenic sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050057
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  • 4
    Electronic Resource
    Electronic Resource
    Membrane-associated carbonic anhydrase IV in skeletal muscle: subcellular localization (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 405-411 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Carbonic anhydrase IV (CA IV) was examined by light microscopy and electron microscopy in rat soleus muscle. Semithin sections of aldehyde-fixed Epon-embedded muscle were stained with rabbit anti-rat lung CA IV and the avidin-biotin-peroxidase complex. With this technique, capillaries and sarcolemma showed positive CA IV staining. For electron microscopy, rat soleus specimens were aldehyde-fixed, with or without subsequent osmication, and embedded in Epon. Ultrathin sections were immunostained with anti-rat lung CA IV/immunogold. Omitting osmium allowed ample antigen-antibody reactions but could not prevent the release of glycosylphosphatidylinositol-anchored CA IV from the membranes, which led to apparent background staining. Postosmication significantly reduced tissue antigenicity but kept the antigen bound to the membranes and thus allowed a very precise localization of CA IV. By electron microscopy, membrane-bound CA IV is found to be associated with capillary endothelium, sarcolemma, and sarcoplasmic reticulum (SR). Conceivably, the presence of SR staining in ultrathin sections and its absence in semithin sections reflect a problem of accessibility of the antigenic sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02473299
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  • 5
    Electronic Resource
    Electronic Resource
    Diffusion of myoglobin in skeletal muscle cells — dependence on fibre type, contraction and temperature (1995)
    Springer
    Pflügers Archiv 430 (1995), S. 519-525 
    Details
    ISSN: 1432-2013
    Keywords: Diffusion coefficient ; Muscle cells ; Myoglobin ; Microinjection ; Oxygen ; Facilitated diffusion ; Intracellular oxygen transport ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We measured the diffusion coefficient of myoglobin (D Mb) inside mammalian skeletal muscle cells with a microinjection technique. A small bolus of horse Mb was injected into a single muscle fibre and the subsequent time-dependent changes of the Mb profiles along the fibre axis were measured with a microscope-photometer. For fibres of the rat soleus muscle at 22° C, a D Mb of 1.3·10−7 cm2/s was found, confirming a result obtained previously by us for rat diaphragm muscle with a photo-oxidation technique. In the extensor digitorum longus muscle of the rat, a higher value of 1.9 · 10−7 cm2/s was measured. Auxotonic muscle contractions did not change the apparent D Mb. For the temperature range between 22 ° C and 37 ° C, a temperature coefficient, Q 10, of 1.5 was calculated. The implication of this result for the role of Mb in the facilitation of oxygen transport was examined. Model calculations show that with this relatively low D Mb value, the intracellular oxygen supply can be improved only slightly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00373888
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  • 6
    Electronic Resource
    Electronic Resource
    A rapid electrophoretic method for separating rabbit skeletal muscle myosin heavy chains at high resolution (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 64-66 
    Details
    ISSN: 0173-0835
    Keywords: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis ; Myosin heavy chains ; Adult isomyosin ; Developmental isomyosin ; Rabbit skeletal muscle ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: An electrophoretic method using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was developed which gives a high-resolution separation of the known myosin heavy chains of rabbit skeletal muscle with excellent reproducibility. The gel of 10 cm total length consists of (i) a first stacking gel of 3.5% total gel concentration (T) and pH 6.8, (ii) a first separating gel of 6.6%T and pH 8.8, (iii) a second stacking gel of 6.6%T and pH 6.8, and (iv) a second separating gel of 8.8%T and pH 8.8. With this composition, a minigel system allows separation of six myosin heavy-chain (MHC) isoforms at room temperature without cooling and within 8h. In agreement with previous reports, the isoforms appear in the sequence MHCemb, MHC IIa, MHC IId, MHCneo, MHC IIb, MHC I. A special advantage is the detectability not only of the adult but also of the embryonic and neonatal isoforms MHCemb and MHCneo.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180113
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