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  • 1
    Electronic Resource
    Electronic Resource
    Effects of Sodium and Bicarbonate Ions on γ-Aminobutyric Acid Receptor Binding in Synaptic Membranes of Rat Brain (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: Crude synaptic membranes treated with Triton X-100 (TX) bound γ-aminobutyric acid (GABA) to two classes of receptor site in Na+-free 10 mM-Tris-sulfate buffer (pH 7.4), but to only a single class of receptor site in 10 MM Tris-sulfate buffer (pH 7.4) containing 150 mM-NaCl. The high-affinity receptor site in TX membranes was specifically masked in the presence of Na+. However, TX membranes incubated in Krebs-Ringer bicarbonate solution (pH 7.4) bound GABA to two classes of receptor site despite the presence of Na+. It was found that addition of bicarbonate ions to the Na+-containing 10 mM-Trissulfate buffer (pH 7.4) could restore the high-affinity class of GABA receptors, rendering both classes detectable. This finding suggests that both Na+ and HCO-3 may have a regulatory function on GABA binding to the receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb00471.x
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  • 2
    Electronic Resource
    Electronic Resource
    Influence of Sodium-Independent γ-Aminobutyric Acid Binding on the Assay of Sodium-Dependent γ-Aminobutyric Acid Binding in a Membrane Preparation of Rat Brain (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: A large amount of [3H]GABA was bound to crude synaptic membrane fractions of rat. by sodium-independent process in a medium that contained 100 μM [3H]GABA used for assaying GABA uptake site. This [3H]-GABA binding was different from receptor binding of GABA. It was confirmed that this sodium-independent [2H]GABA binding scarcely occurred in the presence of a physiological concentration of sodium chloride, and that sodium-independent GABA binding had a negligible influence on sodium-dependent GABA binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb02413.x
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  • 3
    Electronic Resource
    Electronic Resource
    4-Aminobutyraldehyde as a Substance Convertible In Vivo to GABA (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: [2,3-3H]4-Aminobutyraldehyde ([3H]ABAL) was injected subcutaneously into mice, which were sacrificed at various intervals following injection. [3H]γ-Aminobutyric acid ([3H]GABA) synthesized in vivo from [3H]ABAL was extracted from the brains, separated, and quantitated. The results showed that in the brain, injected [3H]ABAL was rapidly transformed into [3H]GABA. [3H]ABAL may penetrate the blood-brain barrier into the central nervous system and then be oxidized to [3H]GABA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb12686.x
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  • 4
    Electronic Resource
    Electronic Resource
    4-Aminobutyraldehyde Dehydrogenase Activity in Rat Brain (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: An enzyme with NAD+-dependent 4-aminobutyraldehyde dehydrogenase activity was purified about 360-fold from rat brain extract. AMP-Sepharose chromatography was effective in separating the enzyme from other NAD+-dependent aldehyde dehydrogenases included in the extract. The Kms for the substrates NAD+ and 4-aminobutyraldehyde were 4.8 × 10−4 and 8.3 × 10−5M, respectively. The pH optimum for the enzyme was about 8.0. The ratio of activities toward 4-aminobutyraldehyde, propionaldehyde, succinate semialdehyde, and benzaldehyde was 1.00:0.17:0.24:0.09:0.03 when the activity toward 4-aminobutyraldehyde was set equal to 1.00. The enzyme activity in subcellular fractions of rat brain was localized in cytosol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb07963.x
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of γ-Aminobutyric Acid Binding Sites on Crude Synaptic 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: [3H]GABA binding to crude synaptic membranes of rat brain was studied in an attempt to identify GABA binding to its synaptic receptor in the presence of Na+. Membrane vesicles prepared from crude synaptic membrane fractions were useful as a tool to differentiate synaptic GABA receptors from GABA uptake sites. The crude synaptic membranes treated with Triton X-100 [membranes (TX)] involved two classes of GABA binding sites (KD= 38.7 and 78.0 nM) in the absence of Na+, but the high-affinity sites disappeared in the presence of Na+ and a single class of GABA binding sites (KD= 75.0 nM) was detected. The failure to detect an active uptake of [3H]GABA into the vesicles prepared from membranes (TX) suggests that the [3H]GABA binding in the presence of Na+ was related to synaptic GABA receptors. It is probable that Na+ could mask the presence of the high-affinity class of GABA receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb00453.x
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  • 6
    Electronic Resource
    Electronic Resource
    Analysis and separation of synaptosomal membrane proteins (1990)
    Springer
    Neurochemical research 15 (1990), S. 475-481 
    Details
    ISSN: 1573-6903
    Keywords: Synaptosomes ; membrane proteins ; two-dimensional electrophoresis ; reversed-phase HPLC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Synaptosomal membrane proteins solubilized with 8% CHAPS-8 M urea were analyzed with twodimensional electrophoresis (2DE). The membrane proteins were resolved up to 250 spots on a 2DE map, ranging in isoelectric points (pI) from 3.5 to 10.0 and molecular weights (MW) from 10 kDa to 200 kDa. Comparison of the mapped proteins of synaptosomal membranes with those of myelin and mitochondorial membranes revealed that synaptosomal membrane proteins were characteristic in the area of pI from 4.0 to 7.5 and MW from 20 kDa to 130 kDa, and that at least 30 spots were synaptosomal membrane-specific proteins. Most of these 30 proteins have not been previously described, named, and characterized Serial numbers (from SY1 to SY30) were assigned to the proteins on the map in order to investigate them systematically. A preliminary attempt to separate synaptosomal membrane proteins was carried out using a reversed-phase HPLC system. Several proteins could either be isolated or enriched. SY10 (pI 4.6; MW 56 kDa) was one of these proteins, and was of particular interest for its unusual behavior on the reversed-phase column, and for its binding to an immobilized protein A-gel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00966203
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  • 7
    Electronic Resource
    Electronic Resource
    Analysis of Con A-binding glycoproteins in synaptosomal membranes (1992)
    Springer
    Neurochemical research 17 (1992), S. 1011-1014 
    Details
    ISSN: 1573-6903
    Keywords: Synaptosomes ; membrane glycoproteins ; Con A-binding ; protein A-binding ; two-dimensional electrophoresis ; immunoglobulin supergene family
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Concanavalin A (Con A)-binding proteins obtained from solubilized synaptosomal membranes of bovine brain were analyzed by two-dimensional electrophoresis (2DE), and were identified by peroxidase conjugated Con A (Con A-peroxidase staining), after transfer from 2DE gel to nitrocellulose paper. The Con A-binding proteins were resolved up to 40 spots, ranging in isoelectric points (pI) from 4.5 to 8.0 and molecular weight (MW) from 10 kDa to 120 kDa. Most of the Con A-binding proteins were streaked across a pH gradient and/or exhibited as multiple spots, indicating broad charge and molecular weight heterogeneity. The presence of protein groups that showed high affinities for Con A were revealed. Most interesting group (named GP51), which consisted of seven spots separated horizontally in charge heterogeneity (pI5.85-7.5) with MW 51kDa, was characterized by its binding to an immobilized protein A gel. This implies that GP51 is related to immunoglobulins and/or GP51 may be a new member of the immunoglobulin supergene family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00966829
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  • 8
    Electronic Resource
    Electronic Resource
    Detection of abnormal haemoglobin by capillary electrophoresis and structural identification (1992)
    New York, NY : Wiley-Blackwell
    Biomedical Chromatography 6 (1992), S. 224-226 
    Details
    ISSN: 0269-3879
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Haemoglobin obtained from a male adult Ghanian with retinopathy, which was probably caused by haemoglobinopathy was analysed by capillary electrophoresis (CE) for clinical diagnosis. Two major peaks, which were in the ratio of nearly one, were detected. The elution times of these peaks (HbXI and HbXII) were faster than that of normal haemoglobin (HbA). The existence of two different abnormal types of haemoglobin was clear in the patient blood. The following sequence analysis revealed that the first peak (HbXI) was HbC and the second (HbXII) was HbS on the electropherogram, and that the patient was a heterozygote of HbS and HbC (HbSC disease). One of the diagnostic processes in a haemoglobin disease was shown by the combined use of CE, HPLC and a protein sequencer.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bmc.1130060504
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  • 9
    Electronic Resource
    Electronic Resource
    Assay of vitamin B6 in human plasma with graphitic carbon column (1993)
    New York, NY : Wiley-Blackwell
    Biomedical Chromatography 7 (1993), S. 162-165 
    Details
    ISSN: 0269-3879
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A high performance liquid chromatographic (HPLC) procedure for measuring pyridoxal-5′-phosphate (PLP) and certain forms of B6 vitamers in plasma is presented here. This HPLC procedure consisted of a single graphitic carbon column with a fluorescence detector employing an isocratic eluent (15% acetonitrile:1% perchloric acid: 0.05% sodium bisulfite). The graphitic carbon column is useful in acidic eluent without deteriorization. The relatively low fluorescent intensity of PLP under acidic conditions is improved by its derivatization with bisulfite in the eluent during chromatographic separation. Using this procedure, the detection limit of PLP is 50 fmol, and an aliquot of 5-50 μL of human plasma is required giving satisfactorily precise results within 5 min. We applied this method to the determination of PLP and certain B6 vitamers in human plasma after oral supplementation of pyridoxine.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bmc.1130070313
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  • 10
    Electronic Resource
    Electronic Resource
    Isolation of intramitochondrial helical filaments appearing in outer compartment of mitochondria (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 241 (1995), S. 149-154 
    Details
    ISSN: 0003-276X
    Keywords: Mitochondria ; Helical filaments ; Hepatocytes ; Ethanol ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Background: Packets of helical filaments have been observed in the outer compartment of occasional mitochondria in many cell types in a variety of animals. The compositon and funcation of these intramitochondrial helical filaments (IMHF) are unknown.Methods: IMHF wre induced in a hepatic mitochondria by administration of ethanol in the drinking water of rats. Hepatic mitochondria were isolated and ruptured by osmotic shock, relasing their IMHF. To purify these structures, the IMHF-containing supernatant was further fractionated by ammonium sulfate precipitation, a 50-60% solution of this reagent being the most effective in this regard. Isolated IMHF were examined by electron microcopy and were analyzed by SDS-PAGE.Result Isolated IMHF closely resembled their in situ counterparts: they had a right-handed helical structure with a 16 nm pitch. SDS-PAGE analysis revealed that they contained three polypeptides with weigh tmolecular of 135, 98, and 53 kD, respectively.Conculusions: These observations will stand as a aseline for comparisons with IMHF that occur naturally or that are induced in other cell types by other kinds of experimental manipulation. © 1995 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092410202
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