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  • 1980-1984  (6)
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Material
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Enzymatic Detyrosination of Tubulin Tyrosinated in Rat Brain Slices and Extracts (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 38 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Tubulin was tyrosinated in slices and in extracts of brain of rats of 3, 25, and 120 days of age by successive incorporation of [14C]tyrosine and [3H]-tyrosine, respectively. The release of the incorporated amino acid was measured by using tubulinyl-tyrosine carboxypeptidase, carboxypeptidase A, and tubulin-tyrosine ligase. With the carboxypeptidases no differences in either the rates or the extents of the release of tyrosine between these two differently labeled tubulins were found. Differences were found when the detyrosination was catalyzed by the ligase and these were attributed to a higher inactivation of tubulin labeled in slices than of that labeled in extracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb10860.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis of Retinal Gangliosides During Chick Embryonic Development (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 35 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Embryonic retina cells incorporated radioactivity from D-[6-3H]glucosamine into gangliosides in vitro. The incorporation was higher in retinas from younger embryos. The pattern of labeling of individual gangliosides of the retina changed gradually from a predominant labeling of gangliosides running chromatographically as GD3 (nomenclature of Svennerholm) and GM3 in retinas from 8-day-old embryos to a predominant labeling of those running as GDIa and GT, in retinas from 13–18-day-old embryos and newly hatched chicks. The shift in the pattern of labeling correlated with a temporary increase of about sixfold of the activity of UDP-N-acetyl-galactosamine:GM3 N-acetylgalactosaminyltransferase occurring between days 8 and 14 of embryonic development and with a regular increase of the activity of the UDP-galactose:GM2 galactosyltransferase occurring from day 8 until hatching. The activities of the CMP-NeuAc:lactosylceramide-, CMP-NeuAc:GM3-, and CMP-NeuAc:GM1-sialosyltransferases in the retinas of newly hatched chicks were 40, 20, and 40%(in comparison with the corresponding activities determined in retinas of the 8-day-old embryo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb12494.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Tubulinyl-tyrosine Carboxypeptidase from Chicken Brain: Properties and Partial Purification (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 34 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Tyrosine can be released from tubulinyl-tyrosine by the action of a brain carboxypeptidase. The molecular weight of this enzyme found by gel filtration through a column of Sephadex G-200 was 90,000. The enzyme was very unstable in a purified preparation in which the activity per milligram of protein was increased 250-fold with respect to the starting material. The precise magnitude of the purification cannot be stated because of the unknown amount of endogenous tubulinyl-tyrosine in the material to be assayed. A comparative study was done between tubulinyl-tyrosine carboxypeptidase (TTCP) activity and pancreatic carboxypeptidase A (CPA, EC 3.4.12.2) activity using tubulinyl-[14C]tyrosine as substrate. The most remarkable differences found are: MgCl2 (2 mM), phenyl acetate (10 mM), or EDTA (5 mM) increased the TTCP activity whereas the CPA activity was strongly inhibited by these compounds, lodoacetate (2 mM) and ZnCl2 (0.1 mM) inhibited the TTCP activity more than the CPA activity. Contrarily, mercaptoethanol (50 mM) and dimethyl sulfoxide (5%) showed a stronger inhibitory effect on CPA than on TTCP. Of several N-carbobenzoxy dipeptides (Z-dipeptides) tested the greatest inhibitory effects on TTCP activity were obtained with Z-Glu-Tyr and Z-Glu-Phe, although strong inhibitory effects on CPA were also obtained with other Z-dipeptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb04628.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Disposition of Gangliosides and Sialosylglycoproteins in Neuronal Membranes (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 37 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract Labeled gangliosides and glycoproteins were obtained by incubation of homogenized neuronal perikarya from rat brain with CMP-[3H]N-acetyl neuraminic acid. The highest degree of labelling was observed in a subcellular fraction that also showed the highest specific activities for several ganglioside glycosyltransferases. The [3H] sialosylglycoconjugates of this fraction remained associated with the membranes after treatment with 1 m-KCl, 125 mm-EDTA, repeated freezing and thawing, or controlled sonication, but were solubilized by sodium deoxycholate (DOC) at a concentration high enough to solubilize the choline phospholipids. About 75% of the neuraminidase-labile sialosyl residues of these labeled endogenous gangliosides and glycoproteins were protected from the action of added neuraminidase or pronase or both enzymes added together. The protection was not abolished by pretreatment of the membranes with high ionic strength or with EDTA but was abolished by sonication or low concentration of DOC. Between 50 and 80% of the neuraminidase-labile sialosyl residues of the gangliosides of the neuronal perikaryon membrane fraction labeled in vivo by an intracerebral injection of N-[3H]acetylmannos-amine were, at 3 h after the injection, also protected from the action of added neuraminidase. The protection was abolished by the addition of DOC. In contrast with the behavior of the labeled glycoconjugates of this neuronal perikaryon fraction, the gangliosides and sialosylglycoproteins from intact synaptosomes were accessible to neuraminidase. It is suggested that most gangliosides and sialosylglycoproteins are sialosylated as intrinsic components of the neuronal perikaryon membrane fraction and that at some stage of the process of transport through the axon and incorporation into the synaptic plasma membrane they change their accessibility to added enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb04466.x
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Inhibition of the UDP-N-Acetylgalactosamine: GM3, N-Acetylgalactosaminyl Transferase by Gangliosides (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Gangliosides in the range of 0.1–0.4 mM inhibited the UDP-N-acetylgalactosamine:GM3, N-acetyl-galactosaminyl transferase (EC 2.4.1.79) of chicken retina. Other lipids such as phosphatidylethanolamine, sphingomyelin, sulfatides, and phosphatidic acid in concentrations similar to those of gangliosides did not affect the enzyme activity significantly. GM3 has an inhibition capability slightly less than that of gangliosides with two or three sialyl groups in their molecules, while asialo-GM1 is clearly less inhibitory. The inhibitory effect of a constant amount of GT1 ganglioside was higher at low concentrations of membrane preparation, but the inhibition was similar at different concentrations of the substrates GM3 or UDP-N-acetylgalactosamine and at all incubation times studied. The added gangliosides were found attached to the membranes. In this attached state they may act either as substrate or inhibitor. The inhibitory effect of gangliosides was not apparent when a mixture of Triton CF 54-Tween 80 was added to the incubation medium at concentrations 〉0.33%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb02773.x
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Ganglioside-cholera toxin interactions: a binding and lipid monolayer study (1982)
    Springer
    Molecular and cellular biochemistry 46 (1982), S. 155-160 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary On t.l.c. plates 125I-cholera toxin binds to a disialoganglioside tentatively identified as GDlb with about 10 times less capacity than to ganglioside GM1. Binding of labeled toxin to both gangliosides was abolished in presence of excess amounts of unlabeled B subunit. Ganglioside extracts from human or pig intestinal mucosa showed toxin binding to gangliosides GM1 and GD1b. In ganglioside-containing lipid monolayers the penetration of the toxin was independent of the ganglioside binding capacity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00239664
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    Paper (German National Licenses)
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