Library

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
Filter
  • 1980-1984  (11)
Source
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    IMMUNOELECTRON MICROSCOPIC LOCALIZATION OF ACYL-CoA OXIDASE IN RAT LIVER AND KIDNEY (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 386 (1982), 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.1749-6632.1982.tb21460.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of two peroxisomal enzymes of lipid β-oxidation in specific granules of rat eosinophils (1983)
    Springer
    Histochemistry and cell biology 78 (1983), S. 425-433 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Peroxisomes contain a system for β-oxidation of fatty acids which differs from the mitochondrial system and is associated with hydrogen peroxide formation. We show that two enzymes: enoyl-CoA hydratase and 3-ketoacyl-CoA thiolase of the peroxisomal system are present in specific granules of rat eosinophils. Both enzyme proteins were pufiried from rat liver and monospecific antibodies were raised in rabbits. Eosinophils from peripheral blood and tissue eosinophils from the wall of intenstine, fixed by glutaraldehyde and embedded in Epon were investigated. The postembedding immunocytochemical procedure with protein A-gold technique was used. The gold particles representing the antigenic sites for both enzymes were present only in specific granules of eosinophils with no immune deposits in mitochondria, nucleus and the cytoplasm. Although gold particles were found over the entire domain of the granule, the electron dense paracrystalline inclusions contained more gold than the granule matrix. Control preparations incubated with nonspecific IgG and protein A-gold complex alone were negative. These findings indicate that in specific granules of eosinophils both peroxisomal and lysosomal enzymes share the same intracellular compartment. The peroxisomal lipid β-oxidation in eosinophils may be involved in generation of hydrogen peroxide, which has a crucial role in killing of metazoon parasites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00496194
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Fine localization of serine: pyruvate aminotransferase in rat hepatocytes revealed by a post-embedding immunocytochemical technique (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 591-595 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunocytochemical localization of serine: pyruvate aminotransferase (SPT) in rat hepatocytes was studied using a protien A-gold technique. Rat liver was fixed by perfusion. Vibratome sections (100 μm thick) of the liver were embedded in Epon or Lowicryl K4M. Ultrathin sections were incubated with antiSPT, followed by protein A-gold complex. Gold particles representing the antigenic sites for SPT were seen in three subcellular compartments, peroxisomes, mitochondria, and cytoplasm. In the control experiments the specificity of the immunolabelling was confirmed. Quantitative analysis of the labelling density showed that main subcellular compartments containing SPT are mitochondria and peroxisomes. In addition, the gold particles distributing in the cytoplasm were 16%–29% of the total labelling. The result indicated that the cytoplasm also contains SPT with a low density.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553722
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Innermembrane association of three mitochondrial β-oxidation enzymes revealed by immunoelectron microscopic technique (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 547-552 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Ultrastructural localization of three mitochondrial β-oxidation enzymes, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and 3-ketoacyl-CoA thiolase in rat liver was studied by a post-embedding immunocytochemical technique. Rat liver was fixed by perfusion. Vibratome sections (100 μm thick) were embedded in Lowicryl K4M. Ultrathin sections were separately incubated with antibody to each enzyme, followed by protein A-gold complex. Gold particles representing the antigenic sites for all enzymes examined were confined exclusively to mitochondria of hepatocytes and other sinus-lining cells. Peroxisomes were consistently negative for the immunolabelling. In the mitochondria the gold particles were localized in the matrical side of inner membrane. The control experiments confirmed the specificity of the immunolabelling. The results firstly indicate that the mitochondrial β-oxidation enzymes are present in the matrix of mitochondria and associated with the inner membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553715
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Immunoelectron microscopic localization of albumin in smooth and striated muscle tissues of rat (1982)
    Springer
    Histochemistry and cell biology 74 (1982), S. 379-386 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Localization of serum albumin in the striated and smooth muscles of rat was studied by an improved immunocytochemical method. Diaphragm, ventricular myocardium, and smooth muscle of stomach were examined. In all of these tissues, albumin was found in the interstitial space and small subsarcolemmal caveolae and vesicles. In addition, the transverse tubular system of the striated muscle stained positive for albumin. The subsarcolemmal vesicles containing albumin did not show any evidence of fusion with lysosomes. Furthermore, in smooth muscle, most of these vesicles were open to the extracellular space. These results demonstrate that albumin in smooth and striated muscle is confined to the extracellular space suggesting that substances such as fatty acids which are carried by albumin are split from it and taken up at the level of the plasma membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493437
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Immunoelectron microscopic localization of cathepsin D in lysosomes of rat nerve cells (1983)
    Springer
    Histochemistry and cell biology 79 (1983), S. 345-352 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunoelectron microscopic localization of cathepsin D in rat nerve cells was investigated using protein A-gold technique. Brain and spinal cord were fixed by perfusion with 4% paraformaldehyde and 1% glutaraldehyde in 0.05 M cacodylate buffer. Vibratome sections of the cerebellum and spinal cord were embedded in Epon 812 or Lowicryl K4M. The postembedding immunocytochemical procedures with protein A-gold were applied to ultrathin sections. Gold particles representing the antigen sites of cathepsin D were localized in lysosomes of Purkinje cells and of presumed motorneurons in the anterior horn. A few gold particles were in Golgi stacks of these cells. The results indicate that the main subcellular domain for cathepsin D in rat nerve cells is lysosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00491770
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Light microscopic immunocytochemical demonstration of peroxisomal enzymes in epon sections (1984)
    Springer
    Histochemistry and cell biology 81 (1984), S. 15-22 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A procedure is described for light microscopic immunocytochemical localization of catalase and three enzymes of peroxisomal lipid β-oxidation: acyl-CoA oxidase, enoyl-CoA hydratase and 3-ketoacyl-CoA thiolase in semithin sections of rat liver processed for routine electron microscopy. Satisfactory immunostaining required the removal of the epoxy resin with sodium ethoxide, controlled digestion of deplasticized sections with proteases and, in case of osmiumfixed tissue, bleaching with oxidants. Resin removal was essential for successful immunostaining, and protease treatment enhanced markedly the intensity of the reaction. This study shows that tissues processed for conventional ultrastructural studies can be used for postembedding immunocytochemical demonstration of various peroxisomal enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495395
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Innermembrane association of three mitochondrial β-oxidation enzymes revealed by immunoelectron microscopic technique (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 547-552 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Ultrastructural localization of three mitochondrial β-oxidation enzymes, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and 3-ketoacyl-CoA thiolase in rat liver was studied by a post-embedding immunocytochemical technique. Rat liver was fixed by perfusion. Vibratome sections (100 μm thick) were embedded in Lowicryl K4M. Ultrathin sections were separately incubated with antibody to each enzyme, followed by protein A-gold complex. Gold particles representing the antigenic sites for all enzymes examined were confined exclusively to mitochondria of hepatocytes and other sinus-lining cells. Peroxisomes were consistently negative for the immunolabelling. In the mitochondria the gold particles were localized in the matrical side of inner membrane. The control experiments confirmed the specificity of the immunolabelling. The results firstly indicate that the mitochondrial β-oxidation enzymes are present in the matrix of mitochondria and associated with the inner membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02400970
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Immunoelectron microscopic localization of serine: Pyruvate aminotransferase in rat eosinophile leukocytes (1983)
    Springer
    Histochemistry and cell biology 78 (1983), S. 417-424 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Localization of serine: pyruvate aminotransferase [EC 2.6.1.51]; SPT in rat eosinophile leukocytes was investigated by protein A-gold technique. Thin sections of rat intestine were incubated with anti-SPT, followed by protein A-gold complex. Labelling with gold particles was seen on the specific granules of eosinophile leukocytes, in which 78% of the gold particles were localized on their paracrystalline cores and 22% on matrix, indicating that the main intragranular sites of SPT are the core. Other cell organelles such as nucleus and mitochondria were not labelled specifically. Quantitative analysis of labelling density in the subcellular compartments also comfirmed that SPT is present exclusively in the specific granules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00496193
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Fine localization of serine: pyruvate aminotransferase in rat hepatocytes revealed by a post-embedding immunocytochemical technique (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 591-595 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Immunocytochemical localization of serine: pyruvate aminotransferase (SPT) in rat hepatocytes was studied using a protien A-gold technique. Rat liver was fixed by perfusion. Vibratome sections (100 μm thick) of the liver were embedded in Epon or Lowicryl K4M. Ultrathin sections were incubated with antiSPT, followed by protein A-gold complex. Gold particles representing the antigenic sites for SPT were seen in three subcellular compartments, peroxisomes, mitochondria, and cytoplasm. In the control experiments the specificity of the immunolabelling was confirmed. Quantitative analysis of the labelling density showed that main subcellular compartments containing SPT are mitochondria and peroxisomes. In addition, the gold particles distributing in the cytoplasm were 16%–29% of the total labelling. The result indicated that the cytoplasm also contains SPT with a low density.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02400977
    Library Location Call Number Volume/Issue/Year 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...