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  • 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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  • 2
    Electronic Resource
    Electronic Resource
    THE SITE OF SYNTHESIS OF GANGLIOSIDES IN THE CHICK OPTIC SYSTEM (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 33 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract– In the retinas of 1-day-old chickens that received an intraocular injection of N-[3H]acetylmannosamine the labelling of N-acetylneuraminic acid and CMP-N-acetylneuraminic acid increased for at least 8 h and that of gangliosides for at least 24 h after injection. In the optic tectum contralateral to the injected eye at 8 h after the intraocular injection, the labelling of gangliosides exceeded the labelling of gangliosides in the ipsilateral tectum by approx 20-fold. In the contralateral tectum the highest concentration of labelled gangliosides was in subfractions enriched in synaptosomes and synaptic plasma membranes. No significant contralateral ipsilateral differences were found in the acid soluble substances of the tectum. In the optic tectum, labelled gangliosides appeared earlier in the neuronal perikarya than in synaptosomes when the injection was intracranial. Conversely, when the injection was intraocular the labelling appeared earlier in the synaptosomes than in the neuronal perikarya. The radioactivity pattern of the optic tectum gangliosides resembled the pattern of retina gangliosides when N-[3H]acetylmannosamine was injected intraocularly, but when N-[3H]acetylmannosamine was given intracerebrally the radioactivity pattern resembled that of optic tectum gangliosides. Intraocular injection of colchicine or vinblastine did not affect the labelling of retinal gangliosides from N-[3H]acetylmannosamine injected into the same eye but prevented the appearance of labelled gangliosides in the optic tectum. In vitro the ganglioside glycosylating activity of optic tectum synaptosomes and synaptic plasma membranes was between 6 and 10-fold lower than that found in the optic tectum neuronal perikarya. These findings support the notion that the main subcellular site of synthesis of neuronal gangliosides is in the neuronal perikarya, from which they are translocated to the nerve endings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb09912.x
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  • 3
    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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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    GLYCOPROTEINS AND GLYCOLIPIDS OF SUBCELLULAR FRACTIONS FROM BOVINE RETINA. INCORPORATION OF MANNOSE AND SIALIC ACID (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 28 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Endogenous lipids and proteins of bovine retina subcellular fractions were labelled from CMP-[3H]NeuNAc and GDP-[14C]mannose. The bulk of NeuNAc and mannose transfer activity was in membranes other than those from the rod outer segment (ROS). Lighter and heavier membranes, obtained from ROS free membranes by density gradient centrifugation, were the most active for the incorporation of NeuNAc and mannose, respectively. NeuNAc bound to a lipid indistinguishable from gangliosides, and a lipid that contains mannose (mannolipid-I) were found in the fraction extractable with chloroform-methanol (2:1, v/v). Mannose was also incorporated into a lipid fraction extractable with chloroform-methanol-water (1:1:0.3, by vol) (mannolipid-II). Mannolipid-I and mannolipid-II were labile to mild acid hydrolysis. In the presence of ROS free membranes, radioactivity of mannoli-pid-I was transferred to mannolipid-II and from this to proteins. Analyzed by sodium dodecyl sulphate polyacrylamide gel electrophoresis, the proteins labelled from GDP-mannose migrated as a broad peak covering the range of molecular weights 20,000–30,000 and including the zone of rhodopsin migration. The proteins labelled from CMP-NeuNAc showed four radioactive peaks that were coincident with three out of four periodic acid-Schiff (PAS) positive bands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10631.x
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  • 6
    Electronic Resource
    Electronic Resource
    Split chromatographic spot produced by supposedly single gangliosides treated with trichloroacetic acid—phosphotungstic acid reagent (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 26 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb04467.x
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  • 7
    Electronic Resource
    Electronic Resource
    CAPACITIES FOR BINDING AMINO ACIDS BY tRNAs FROM RAT BRAIN AND THEIR CHANGES DURING DEVELOPMENT (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: –The total tRNA and some specific tRNAs from the 100,000g soluble fraction of rat brain were measured during development (postnatal ages 4–55 days). For determination of specific tRNAs we developed a method that measured their capacities to bind specific amino acids. Levels of total tRNA were decreased in the soluble fraction from the brains of 55-day-old rats in comparison to those for the 4-day-old rats. The aminoacylation capacities of tRNAs for phenylalanine, lysine, proline, valine, leucine, alanine and isoleucine were diminished in the 55-day-old rats in comparison to those for 4-day-old rats when expressed per unit wet weight of brain. When the 4- to 55-day changes in aminoacylation capacity of each specific tRNA was expressed relative to that of the total tRNA, tRNAPhe and tRNALysLys were diminished; tRNAPro, tRNAVel, tRNAGIY and tRNALeu showed no significant changes; and tRNAA1a and tRNAIle were increased. Incorporation of amino acids into a material insoluble in hot TCA (probably proteins) in a ribosome-free system occurred in the brain preparations. Out of ten different amino acids studied, arginine and tyrosine exhibited the highest values for this type of transfer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01282.x
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  • 8
    Electronic Resource
    Electronic Resource
    A SOLUBLE PREPARATION FROM RAT BRAIN THAT INCORPORATES INTO ITS OWN PROTEINS [14C]ARGININE BY A RIBONUCLEASE-SENSITIVE SYSTEM AND [14C]TYROSINE BY A RIBONUCLEASE-INSENSITIVE SYSTEM (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— A 100,000 g supernatant fraction from rat brain that was passed through a column of Sephadex G-25-40 was able, after addition of some factors, to incorporate [I4C]arginine (apparent Km= 5 μM) and [14C]tyrosine (apparent Km= 20 μM) into its own proteins. The factors required for the incorporation of [14C]arginine were: ATP (optimal concentration = 0-25-2 μM) and Mg2+ (optimal concentration 5 mM). For the incorporation of [I4C]tyrosine the required factors were: ATP (apparent Km= 0-75 μM), Mg2+ (optimalconcentration 8-16 mM) and K+ (apparent Km= 16 mM). Addition of 19 amino acids did not enhance these incorporations. Optimal pHs were: for [14C]arginine and [14C]tyrosine, respectively, 7-4 and 7-0 in phosphate buffer and 7–9 and 7-3-8-1 in tris-HCl buffer. Pancreatic ribonuclease abolished the incorporation of [14C]arginine but had practically no effect in the incorporation of [14C]tyrosine. Furthermore, [14C]arginyl-tRNA was a more effective donor of arginyl groups than [14C]arginine, whereas [14C]tyrosyl-tRNA was considerably less effective than [14C]tyrosine. The incorporations of [14C]arginine and [14C]tyrosine into brain proteins were from 25- to 2000-fold higher than for any other amino acid tested (12 in total). In brain [14C]arginine incorporation was higher than in liver and thyroid but somewhat lower than in kidney. In comparison to brain, the incorporation of [14C]tyrosine was negligible in liver, thyroid or kidney. Kinetic studies showed that the macromolecular factor in the brain preparation was complex. The protein nature of the products was inferred from their insolubilities in hot TCA and from the action of pronase that rendered them soluble. [14C]Arginine was bound so that its a-amino group remained free. Maximal incorporation of [14C]tyrosine in brain of 30-day-old rats was about one-third of that in the 5-day-old rat. The changes with postnatal age in the incorporation of [14C]arginine were not statistically significant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb12108.x
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  • 9
    Electronic Resource
    Electronic Resource
    SYNTHESIS OF GANGLIOSIDES DURING DEVELOPMENT AND ITS RELATION TO THE QUANTITATIVE CHANGES OF SUBCELLULAR PARTICLES OF RAT BRAIN (1968)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 15 (1968), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Different subcellular fractions prepared from developing rat cerebrum were quantified by determinations of dried weights and protein contents. It was found that there is an increase of 2–2·5 times in the weights of synaptosomes and mitochondria/g of tissue during the first 20 days of extrauterine life.A period of fast synthesis of gangliosides, with a similar pattern of increase for the different subcellular particles, was found during the first 15 days of life by study of the incorporation of injected d-[1-14C]glucosamine in rats at different stages of development. Attempts to find out if gangliosides from a certain fraction are precursors of those of other fractions indicated that in all fractions the gangliosides increase independently of the other fractions. It is concluded that the enzymic systems of synthesis of these glycolipids are present in vivo in all the fractions considered.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1968.tb05902.x
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  • 10
    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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