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  • 1
    Electronic Resource
    Electronic Resource
    Glutaminase from pig kidney, an allosteric protein
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 20 (1965), S. 566-572 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0006-291X(65)90436-5
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of anaerobiosis and addition of keto acids on glutamine utilization by Ehrlich ascites-tumor cells
    Amsterdam : Elsevier
    BBA - Biochimica et Biophysica Acta 42 (1960), S. 187-188 
    Details
    ISSN: 0006-3002
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0006-3002(60)90779-4
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  • 3
    Electronic Resource
    Electronic Resource
    Evidence for Compartmentation of Synaptosomal Phosphate-Activated Glutaminase (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Phosphate-activated glutaminase (EC 3.5.1.2) in synaptosomal preparations is inhibited 40–60% by the sulphydryl group reagent N-ethylmaleimide (NEM), forming the basis for distinction between NEM-sensitive and NEM-insensitive glutaminases. The NEM effect cannot be explained by differential effects on distinct glutaminases because other glutaminases have not been detected, and the synaptosomal glutaminase activity can be fully accounted for by the activity of phosphate-activated glutaminase. By fractionation of mitochondria isolated from synaptosomal preparations, which are preincubated with and without NEM, both NEM-sensitive and NEM-insensitive glutaminases are found to be localized to the inner mitochondrial membrane. Variations in pH (7.0–7.6) and the phosphate concentration (5–10 mM) affect chiefly NEM-sensitive glutaminase, demonstrating that this glutaminase may be subject to regulation by compounds in the cytosol having restricted permeability to the inner mitochondrial membrane. Since p-hydroxymercuribenzoate, which is known to be impermeable to the inner mitochondrial membrane, inhibits glutaminase similarly to NEM, phosphate-activated glutaminase is assumed to be compartmentalized within the inner mitochondrial membrane. Thus, NEM-sensitive glutaminase is localized to the outer face and NEM-insensitive glutaminase to the inner region of this membrane and probably also to the matrix region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb10815.x
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  • 4
    Electronic Resource
    Electronic Resource
    HISTAMINE-DEPENDENT FORMATION OF N-ACETYL-ASPARTYL PEPTIDES IN MOUSE BRAIN (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The formation of N-acetyl-aspartyl-peptides in mouse brain homogenates is described. The formation is completely dependent on histamine and on an ATP-regenerating system, and partially dependent on the addition of N-acetyl-aspartate and certain other amino acids. The N-acetyl-aspartyl-peptide formation is probably non-ribosomal and is apparently not due to hydrolysis of preformed proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb07529.x
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  • 5
    Electronic Resource
    Electronic Resource
    ISOLATION OF AN ACID-SOLUBLE PROTEIN WITH LOW MOLECULAR WEIGHT FROM MONKEY BRAIN (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: Abstract— The isolation of a perchloric acid-soluble low molecular weight protein from brain of Macaca irus is reported. Sodium dodecyl sulphate polyacrylamide gel electrophoresis and gel isoelectric focusing indicate that the protein is free of impurities. The molecular weight, as determined by gel filtration and sodium dodecyl sulphate gel electrophoresis, is shown to be 10,400 and 9900, respectively. This is in agreement with the value of 10,700 obtained from amino acid analysis. The protein contains 27 per cent acid amino acids and 15 per cent basic amino acids. However, the relatively high amide content gives the protein a neutral nature as shown by isoelectric point determination using gel isoelectric focusing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01434.x
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  • 6
    Electronic Resource
    Electronic Resource
    EFFECTS OF AMINES ON THE LEVEL OF N-ACETYL-ASPARTATE AND N-ACETYL- ASPARTYL-GLUTAMATE IN MOUSE BRAIN TISSUE SLICES (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The effect of some biogenic amines and amino acids on the level of N-acetyl-asparticacid and N-acetyl-aspartyl-glutamic acid has been investigated in mouse brain tissue slices. The amines all caused a significant decrease in the levels of N-acetyl-aspartic acid and N-acetytl-aspartyl-glutamic acid within 5 min of incubation, while the amino acids, in spite of being possible transmitter candidates, had no such effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb05071.x
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  • 7
    Electronic Resource
    Electronic Resource
    ACETYLATED AND PEPTIDE BOUND GLUTAMATE AND ASPARTATE IN BRAIN (1967)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 14 (1967), 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.1471-4159.1967.tb09510.x
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  • 8
    Electronic Resource
    Electronic Resource
    PURIFICATION OF PHOSPHATE-DEPENDENT PIG BRAIN GLUTAMINASE (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 procedure for preparing highly purified phosphate-activated glutaminase (EC 3.5.1.2, L-glutamine amidohydrolase) from pig brain is described. The main steps consist of extraction with acetone, followed by sodium sulphate fractionation of the solubilized acetone powder. Thereafter, solubilization by dialysis against a buffer containing tris-HC1, mercaptoethanol, and EDTA, followed by precipitation with phosphate-borate, is repeated twice. The final preparation contains no impurities which can be detected by polyacrylamide gel electrophoresis, isoelectric focusing, and sedimentation equilibrium centrifugation. By the latter method, molecular weight is determined to be 187,000. By polyacrylamide gel electrophoresis in sodium dodecyl sulphate, one protein band with molecular weight 64,000 is found.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb00090.x
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  • 9
    Electronic Resource
    Electronic Resource
    PHOSPHATE ACTIVATED GLUTAMINASE ACTIVITY AND GLUTAMINE UPTAKE IN PRIMARY CULTURES OF ASTROCYTES (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Uptake and release of glutamine were measured in primary cultures of astrocytes together with the activity of the phosphate activated glutaminase (EC 3.5.1.2). In contrast to previous findings of an effective, high affinity uptake of other amino acids (e.g. glutamate, GABA) no such uptake of glutamine was observed, though a saturable, concentrative uptake mechanism did exist (Km= 3.3 ± 0.5 mm; Vmax= 50.2 ± 12.6 nmol ± min−1± mg−1). The phosphate activated glutaminase activity in the astrocytes (6.9 ± 0.9 nmol ± min−1± mg−1) was similar to the activity found in whole brain (5.4 ± 0.7 nmol ± min −l± mg−1), which may contrast with previous findings of a higher activity of the glutamine synthetase (EC 6.3.1.2) in astrocytes than in whole brain. The observations are compatible with the hypothesis of an in vivo flow of glutamate (and GABA) from neurons to astrocytes where it is taken up and metabolized, and a compensatory flow of glutamine towards neurons and away from astrocytes although the latter cell type may be more deeply involved in glutamine metabolism than envisaged in the hypothesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb04579.x
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  • 10
    Electronic Resource
    Electronic Resource
    IN VIVO LABELLING OF ACETYL-ASPARTYL PEPTIDES IN MOUSE BRAIN FROM INTRACRANIALLY AND INTRAPERITONEALLY ADMINISTERED ACETYL-l-[U-14C] ASPARTATE (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 29 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Following intracranial and intraperitoneal injection of acetyl-l-[U-14C]aspartate into mice about 5% and 0.7% of the radioactivity, respectively, was recovered from the brain after 30 min.On chromatographic separation of the cationic and anionic compounds on a Dowex 50 column, the former fraction contained about 60% of the radioactivity, predominantly as labelled aspartate and glutamate. The anionic compounds, containing 20% of the labelled compounds, were fractionated in several chromatographic systems and resolved into a great variety of labelled peptidic compounds of which five acetyl-[U14-C]aspartyl peptides, containing two to four amino acids, were purified. One of these, acetyl-aspartyl glutamine, has not previously been found in brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10690.x
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