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  • 1
    Electronic Resource
    Electronic Resource
    Biotin carboxylases in mitochondria and the cytosol from skeletal and cardiac muscle as detected by avidin binding (1993)
    Springer
    Histochemistry and cell biology 100 (1993), S. 415-421 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Biotin carboxylases in mammalian cells are regulatory enzymes in lipogenesis and gluconeogenesis. In this study, endogenous biotin in skeletal and cardiac muscle was detected using avidin conjugated with alkaline phosphatase and applied in high concentrations to muscle sections. The avidin binding was subsequently visualized by histochemical demonstration of the alkaline phosphatase activity. All cardiac muscle cells showed high affinity for avidin with only the nuclei and the intercalated discs remaining unstained. In skeletal muscle a diffuse reaction could be detected in the sarcoplasm of the muscle fibres. A granular reaction was noted in the same fibres that showed activity for succinic dehydrogenase. The specificity of the coloured reaction product in the muscle sections was investigated and is suggested to be caused by avidin binding to biotin moieties in mitochondria and the cytosol. Mitochondrial and cytosolic preparations of skeletal muscle were electrophoresed in sodium dodecyl sulphate gels. After blotting and incubation with conjugated avidin, two bands with molecular weights of 75 kDa and 130 kDa respectively were evident in the mitochondrial preparation. It is suggested that the 75-kDa band represents comigration of the biotin-containing subunits of propionyl-CoA carboxylase and methylcrotonyl-CoA carboxylase. The 130-kDa band may represent the biotin-containing pyruvate carboxylase. In the cytosolic preparation a 270-kDa band was stained in blots that had been incubated with conjugated avidin; this band is suggested to represent acetyl-CoA carboxylase. A 190-kDa cytosolic band might be a cleavage product of acetyl-CoA carboxylase. We propose that using alkaline phosphatase-conjugated avidin it is possible to detect the mitochondrial and cytosolic biotin-dependent carboxylases in striated muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267821
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  • 2
    Electronic Resource
    Electronic Resource
    The complex-type oligosaccharide binding lectin Datura stramonium agglutinin detects type II A muscle fibres in the brachial biceps from man and cat (1997)
    Springer
    Journal of muscle research and cell motility 18 (1997), S. 31-41 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Complex-type oligosaccharides were detected in the sarcoplasm of muscle fibres from cat and human biceps using lectins and anticarbohydrate antibodies. The lectin Datura stramonium agglutinin strongly stained type II A fibres as identified by myosin ATPase activity after alkaline and acid preincubation. In contrast, all muscle fibres showed a moderate coarse granular staining after incubation with Tetracarpidum conophorum agglutinin and Telfairia occidentalis agglutinin which recognize tri-antennary complex glycans poorly bound by D. stramonium agglutinin. Strong sarcoplasmic staining in all muscle fibres was obtained after incubation with an antibody against branched N-acetyllactosamine structure while an antibody against binary 2←3 sialyllactosamine glycans failed to detect the muscle fibres. Treatment of the muscle sections with sialidase prior to incubation with D. stramonium agglutinin did not influence the lectin staining pattern. Staining of blots from electrophoretically separated muscle proteins obtained byhomogenization, solubilization and centrifugation of small muscle pieces showed D. stramonium agglutinin binding to a number of bands ranging from 200 kDa to 30 kDa. No D. stramonium agglutinin positive bands were observed in blots from separated mitochondrial proteins while blots from sarcoplasmic reticulum separated by electrophoresis stained many bands in the range from 200 kDa to 30 kDA. It may be concluded that all muscle fibres inhuman and cat biceps hold intracellular non-sialylated complex-type oligosaccharides and further, that a specific tri-antennary complex-type glycoform is strongly expressed in type II A fibres as recognized by D. stramonium agglutinin. These results indicate a differential glycosylation of certain myofibrillar-associated proteins in muscle fibre types
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018624715326
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  • 3
    Electronic Resource
    Electronic Resource
    Fucose expression in skeletal muscle: a lectin histochemical study (1993)
    Springer
    Journal of molecular histology 25 (1993), S. 619-627 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Binding sites for three fucose specific lectins, Aleuria aurantia agglutinin (AAA), Lotus tetragonolobus agglutinin (LTA) and Ulex europeus I agglutinin (UEA I), were investigated in sections from normal human and rat muscles, in muscle from patients with Duchenne muscular dystrophy (DMD) and in denervated and devascularized rat muscle. In normal human and rat muscle AAA detected fucosylated glycocompounds in the sarcoplasm, sarcolemma, interfibre connective tissue and vascular structures. In normal human muscle addition of fucose to the AAA incubation medium or treatment of the sections with formaldehyde followed by periodic oxidation before lectin incubation strongly inhibited the staining at all sites other than endothelial cells. In normal rat muscle the same staining procedures strongly inhibited the AAA binding at all sites other than the sarcolemma. Incubation with LTA resulted in a diffuse reaction around the vascular structures in rat muscle, while in human muscle a moderate, homogeneous staining was present in all muscle fibres. Treatment of the sections with formaldehyde and periodic acid before incubation with LTA resulted in strongly labelled muscle capillaries in both human and rat muscle. The only elements in the muscle tissues that were stained with UEA I were human endothelial cells. In denervated and devascularized rat muscle incubation with AAA revealed a novel fucose expression that appeared intracellularly in some necrotic fibres. The AAA-positive fucose residues in the sarcolemma of normal muscle fibres that were resistant to periodic acid oxidation could not be shown by AAA in denervated muscle. In DMD muscle a cryptic sarcolemmal fucose expression could be shown with AAA. It is suggested that both the sarcoplasm and sarcolemma of diseased muscle fibres show altered fucose expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00157876
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  • 4
    Electronic Resource
    Electronic Resource
    Binding Properties of the Galactose-detecting Lectin Pseudomonas aeruginosa Agglutinin (PA-IL) to Skeletal Muscle Fibres. Quantitative Precipitation and Precipitation Inhibition Assays (1999)
    Springer
    Journal of molecular histology 31 (1999), S. 485-493 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Pseudomonas aeruginosa agglutinin (PA-IL) staining and the influence of various carbohydrates on lectin binding to muscle sections were investigated quantitatively using a scanning and integrating microspectrophotometre. A strong dose-dependent inhibition of PA-IL staining in the sections was recorded with galabiose (Galα1-4Gal) while lactose (Galβ1-4Glc) had no inhibitory effect. The affinity of PA-IL to Galα1 carbohydrates was studied by ELISA using immobilized glycoconjugates in which Galα1 glycans were attached to bovine serum albumin or ceramide. PA-IL exhibited strong binding to both simple glycoconjugates having a single Galα moiety and to di- and trisaccharides with terminal Galα1 at the non-reducing end. In all cross-sectioned muscle fibres incubated with PA-IL, the staining was present as a honeycomb-shaped network through the entire cytoplasm. Further, a dense punctuate staining could be shown in most fibres. A similar staining pattern was noticed after incubation with a monoclonal antibody against ryanodine receptors and with biotinylated ryanodine suggesting that the network could represent the sarcoplasmic reticulum. Further, Western blots of a sarcoplasmic reticulum preparation showed multiple bands after incubation with PA-IL. It may therefore be proposed that glycoconjugates carrying terminal Galα1 show affinity for PA-IL and are located to the sarcoplasmic reticulum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1003764111659
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  • 5
    Electronic Resource
    Electronic Resource
    A monoclonal anticarbohydrate antibody detecting superfast myosin in the masseter muscle (1995)
    Springer
    Cell & tissue research 283 (1995), S. 85-92 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Masseter muscle ; Limb muscles ; Superfast fibres ; Myosin heavy chains ; Glycosylation ; Galactose ; ATPase ; Cat ; Dog ; Macaca fascicularis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Superfast-contracting muscle fibres (II M) were identified by ATPase staining and after incubation with an antiserum raised against myosin type II M and with an antibody raised against the Galα1–3Galβ1–4GlcNAc structure. II M fibres were present in masseter muscles from cat, dog and Macaca fascicularis but not in limb muscles from the same animals and not in masseter muscles from rat, pig, cow or man. Electrophoresis and staining of blots from myosin preparations showed that the anticarbohydrate antibody detected myosin heavy chains from cat masseter but not myosin heavy chains from cat biceps. The α-galactose specific lectin Griffonia simplicifolia isolectin B4 (GS I B4) did not stain muscle fibres or myosin heavy chains. Therefore, the epitope on myosin heavy chains defined by the anticarbohydrate antibody is presumably not Galα1–3Galβ1–4GlcNAc although the antibody staining was strongly inhibited after absorption by 10 mM of this trisaccharide. Antibody staining of the muscle fibres was totally inhibited by adding 10 mM p-nitrophenyl β-D-glucuronide to the incubation medium. The results thus imply that an anticarbohydrate antibody distinctively detects a carbohydrate epitope specific for myosin in superfast contracting muscle fibres from jaw-closing muscles and confirm that this epitope is not present in other muscle fibre types. This appears to be the first report on differentiated glycosylation among myosin isoforms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050515
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  • 6
    Electronic Resource
    Electronic Resource
    Histochemical studies on genetical control of hormonal enzyme inducibility in the mouse. III. β-Glucuronidase distribution pattern of epididymis in different genotypes (1979)
    Springer
    Journal of molecular histology 11 (1979), S. 205-222 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis This article reports the application of Hayashi's histochemical technique for β-glucoronidase to mouse epididymis. A methodological study. which established optimal conditions for demonstrating the enzyme in this organ, is reported. The distribution pattern of β-glucuronidase is described and correlated with previous data for α-naphtyl acetate esterase. Differences between sites of granular and diffuse reaction product for these two enzymes are recorded. Possible interpretations of these findings in terms of intracellular localization of enzymes are discussed. Studies on different strains reveal regular differences in histochemical organization between mice of various genotypes. Histochemical data which imply androgen inducibility of β-glucuronidase in mouse epididymis are preliminarily noted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01002997
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  • 7
    Electronic Resource
    Electronic Resource
    Lectin binding in skeletal muscle. Evaluation of alkaline phosphatase conjugated avidin staining procedures (1991)
    Springer
    Journal of molecular histology 23 (1991), S. 345-354 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Cryostat sections from rat gracilis muscles were incubated with different biotinylated lectins: Con A (Concanavilin A), WGA (Wheat germ agglutinin), SBA (soybean agglutinin), GS I and GS II (Griffonia simplicifolia agglutinin), LCA (Lens culinaris agglutinin), PNA (peanut agglutinin) and PSA (Pisum sativum agglutinin). The sections were subsequently treated with alkaline phosphatase conjugated avidin. The lectin binding sites were visualized after incubation in substrate media containing: (1) 5-bromo-4-chloro indoxyl phosphate and Nitro Blue tetrazolium or copper sulphate; (2) naphthol AS-MX phosphate or naphthol AS-BI phosphate and various types of diazonium salts; (3) α-naphthylphosphate and Fast Blue BB; (4) β-glycerophosphate according to the method of Gomori. The results obtained with the alkaline phosphatase methods were compared with those seen with a streptavidin-horseradish peroxidase procedure. Several chromogen protocols for visualizing alkaline phosphatase activity showed differences in the ability to detect lectin binding sites. A sarcoplasmic reaction was evident for Con A, GS II, WGA, LCA, and PSA after incubation in the indoxyl phosphate medium. Sarcoplasmic reaction for GS II was also noticed after incubation with naphthol AS-MX Fast Blue BB and β-glycerophosphate. The latter substrate also gave rise to a sarcoplasmic Con A reaction. With the indoxylphosphate tetrazolium salt method some muscle fibres showed a very strong intracellular reaction after incubation with Con A and GS II while the staining intensity was weak in other fibres. The same muscle fibres were stained with PAS. No sarcoplasmic reactions were observed with either naphthol phosphate media or with the diaminobenzidine peroxidase methods. Further, the staining of the muscle fibre periphery, connective tissue, and capillaries was intensified using the indoxyl method. The indoxylphosphate-tetrazolium salt method seems to be suitable for future investigations of lectin binding sites in muscle sections.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01042179
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  • 8
    Electronic Resource
    Electronic Resource
    Identification of capillaries in sections from skeletal muscle by use of lectins and monoclonal antibodies reacting with histo-blood group ABH antigens (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 181-188 
    Details
    ISSN: 1573-4986
    Keywords: muscle capillaries ; blood group carbohydrate antigens ; lectins ; monoclonal antibodies ; histochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract This study was performed to evaluate the application of different lectins and monoclonal antibodies against ABH antigens to detect and characterize carbohydrate structures in capillaries of skeletal muscle from humans and laboratory animals. Blood group specific lectins (Griffonia simplicifolia, Griffonia simplicifolia isolectin B4,Lotus tetragonlobus, Ulex europaeus, andDolichos biflorus) and monoclonal antibodies reacting with histo-blood group carbohydrate antigens belonging to type 1 (Lea) and type 2 (H, A and Ley) chains were used as histological markers for capillaries in sections from skeletal muscle. The material consisted of 20 human masseter muscle biopsies from individuals with known blood types: (eight blood group O, nine blood group A, two blood group B, and one blood group AB) and masseter muscles specimens from different laboratory animals (mouse, rat, rabbit, cat, dog, pig, cow, and macaca monkey). Unfixed sections and an avidin alkaline phosphatase method were used to visualize the specific reaction.Ulex lectin stained capillaries in all human biopsies either strongly or moderately. Strong muscle capillary reaction was observed in biopsies from O, B and AB individuals while capillaries from A individuals were only moderately stained.Griffonia simplicifolia marked capillaries in A, B, and AB individuals andGriffonia simplicifolia isolectin B4 stained capillaries in muscle biopsies from B and AB donors.Dolichos biflorus was a weak marker of muscle capillaries from A individuals. Only capillaries from O individuals were stained with the antibody against H type 2. Capillary reaction was not observed with the other antibodies used.Girffonia simplicifolia was an excellent marker for capillaries in mouse muscle whileGriffonia simplicifolia isolectin B4 is recommended for rat muscles. Periodic acid treatment and subsequentLotus tetragonolobus staining is suitable to visualize capillaries in mouse, rat and pig muscle. Using a sensitive histochemical technique for staining with lectins and monoclonal antibodies reacting with blood group related antigens the microvascular density in human skeletal muscle may be estimated. Further, the carbohydrate compounds in the muscle capillaries reflect the individual blood type. A selection of lectins is suitable for demonstration of capillaries in animal skeletal muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00737716
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  • 9
    Electronic Resource
    Electronic Resource
    The silver staining procedure of sodium dodecyl sulfate-gels may be accelerated by shortening fixation time (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 51-55 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: In most silver staining methods the first step in the staining of proteins separated after sodium dodecyl sulfate-polyacrylamide gel electrophoresis is a rather protracted fixation of the gels. Optimum fixation should be short, cause no background staining and effectively immobilize the proteins in the gel without masking the proteins for reaction with the staining solution. Further, the concentration of the fixing compounds should be as low as possible due to the potentional toxicity of fixatives. Fixation for only 5 min with mixtures of very low concentrations of formaldehyde and glutaraldehyde in ethanol, or a solution of formaldehyde or glutaraldehyde in picric acid and ethanol, fulfill these demands, provided that the gels were prefixed in ethanol-acetic acid for 10 min. As a consequence of these results a fast and sensitive silver staining procedure is proposed.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150140109
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  • 10
    Electronic Resource
    Electronic Resource
    Demonstration of activity for alkaline muscle ATPase in polyacrylamide gels using metal conversion methods (1983)
    Weinheim : Wiley-Blackwell
    Electrophoresis 4 (1983), S. 236-237 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: ATPase activity from skeletal muscle was tested at pH 9.2 in polyacrylamide gels using cobalt or lead conversion techniques. With cobalt it seems that the ion is precipitated both to acrylamide and to certain muscle components resulting in a reproducible but non-enzymatic banding pattern. With the lead technique a specific strongly coloured band is present near the cathode. The band is suppressed by p-hydroxymercuribenzoate but not by levamisole.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150040310
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