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  • 1
    Electronic Resource
    Electronic Resource
    The Isolation of the Mouse Nerve Growth Factor Protein in a High Molecular Weight Form* (1967)
    s.l. : American Chemical Society
    Biochemistry 6 (1967), S. 2202-2209 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00859a043
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  • 2
    Electronic Resource
    Electronic Resource
    STUDIES OF WATER SOLUBLE LIPOPROTEINS IN 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: —The occurrencc of water soluble lipoprotein in the 105,000 g supernatant of rat brain homogenate has been demonstrated.The lipoproteins of brain differed from those of the serum with respect to lipid composition, density and reaction to serum lipoprotein antibodies.Acrylamide gel electrophoresis resolved the brain supernatant into four zones which stained with lipid dye. It was possible to demonstrate that these zones also contained protein by double staining of the gel for lipid and protein. Two of the zones differed in their mobility from serum lipoprotein.Preparative acrylamide gel electrophoresis isolated protein fractions in supematant which contained both lipid and protein and permitted preliminary identification of the lipoprotein bands amongst all the protein bands resolved by acrylamide gel electrophoresis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1968.tb06191.x
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  • 3
    Electronic Resource
    Electronic Resource
    SYNTHESIS OF SULPHATIDE-CONTAINING LIPOPROTEINS IN RAT BRAIN (1969)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 16 (1969), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— 〈list xml:id="l1" style="custom"〉1Puromycin inhibits [14C]leucine Hincorporation into brain proteins, but has no effect on the incorporation of [35S]sulphate into sulphatide. These effects of puromycin are observed not only with the proteins and sulphatide of whole brain, but also with the protein and sulphatide portion of water-soluble lipoprotein complexes.2Microsomes can be separated into three subfractions which differ chemically, morphologically and metabolically. Protein synthesis and sulphatide synthesis are located in different submicrosomal fractions.3The addition of water-soluble brain proteins to the incubation medium causes release of newly synthesized [35S]sulphatide and formation of soluble sulphatide protein complexes. One acceptor protein is identified as the lipoprotein previously shown to bind [35S]sulphatide in vivo (Herschkowitz, McKhann, Saxena and Shooter, 1968b).4These results suggest that protein and sulphatide synthesis can function independently and that association of newly synthesized lipid to preformed protein is possible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1969.tb05949.x
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  • 4
    Electronic Resource
    Electronic Resource
    SOLUTION PROPERTIES OF β NERVE GROWTH FACTOR PROTEIN AND SOME OF ITS DERIVATIVES (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 25 (1975), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The molecular weight of β nerve growth factor protein determined by sedimentation equilibrium in sodium acetate buffer, pH 40, and at protein concentrations around 0-5 mg/ml agrees with the value obtained from the amino acid sequence and confirms the dimeric character of the protein under these conditions. At pH values of 5.0 or greater, β nerve growth factor protein shows either partial dissociation into monomers or aggregation to higher polymers or both phenomena. The extent of dissociation or aggregation depends on buffer type and pH and is most pronounced at alkaline pH. The variation of molecular weight of β nerve growth factor with solvent conditions is similar to that of insulin or proinsulin. Removal of either the two COOH-terminal arginine residues or the two NH2-terminal octapeptide sequences from the protein has no effect on its solution properties at acid pH, the protein remaining a dimer. Species such as 2-5 S nerve growth factor or cyanogen bromide cleaved nerve growth factor which are partically deficient in COOH-terminal arginine residues and/or NH2-octapeptide or nonapeptide sequences are also dimers at pH40. The protein derivative which lacks the two NH2-terminal octapeptide sequence does not, like β-nerve growth factor, display dissociation or aggregation behavior at neutral pH, indicating that these sequences are involved in monomer-monomer interactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1975.tb12243.x
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  • 5
    Electronic Resource
    Electronic Resource
    STUDIES ON THE TURNOVER OF MOUSE BRAIN SYNAPTOSOMAL PROTEINS (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: (l) The half-lives of the proteins of various fractions of whole mouse brain increase with increasing insolubility; the supernatant and hypotonic-extractable proteins had half-lives of about 13 days, whereas the membrane proteins solubilized with Triton X-100 and SLS had half-lives of about 18 days. The proteins of the subfractions of synaptosomes had half-lives ranging from 15 to 19 days; those in the cytoplasm had a half-life of 18·3 days, in the membranes, about 17 days and in the synaptic vesicles, 15·6 days.(2) Although the half-life of the synaptic vesicles was not significantly different from that of other synaptosomal subfractions, the vesicles exhibited a different protein pattern on acrylamide gels, an observation which implies that the proteins of the vesicles are qualitatively different from those of other synaptic membranes.(3) The uptake of labelled lysine into the cytoplasm of the synaptosomes of youg mice in vivo was very rapid.(4) The data derived from the relative specific radioactivities of synaptosomal fractions compared with their whole brain analogs support the contention that a sizeable fraction of the synaptosomal cytoplasmic protein was transported to the synapse by axoplasmic flow. The relative specific radioactivities of synaptosomal membrane and synaptic vesicle proteins rose much more quickly than the comparable activities for the cytoplasmic material, and the alternate possibility of synthesis in situ is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb00184.x
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  • 6
    Electronic Resource
    Electronic Resource
    REGULATION OF NERVE GROWTH FACTOR SYNTHESIS IN MOUSE SUBMAXILLARY GLANDS BY TESTOSTERONE (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 25 (1975), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —It has long been known that the activity of nerve growth factor (NGF) in extracts obtained from the male mouse submaxillary gland is higher than in extracts from the female gland, and that the activity present in female glands can be increased by testosterone treatment. This communication presents a study of the mechanism of the testosterone effect. Of several different steroids administered to female Swiss–Webster mice only testosterone propionate led to increased gland NGF activity. The increase did not appear to be due to an enhancement of the activity of pre-existing molecules on sympathetic nerve fiber outgrowth, or due to an altered affinity for the specific antibodies used in the estimation of NGF content, but appeared rather to be due to an accumulation of NFG molecules. The kinetics of change in the male gland NGF content upon castration and secondary testosterone propionate stimulation was analyzed by application of the plateau principle. The rate of loss of NGF from this organ was not measureably different between the castrate and testosterone propionate stimulated state. On the other hand, there was estimated to be a 10-fold difference in the rate of input between the basal and steroid stimulated state. Tracer amounts of radioiodine labelled NGF administered i.v. was not accumulated by the gland, and there is no evidence for uptake of this protein from the circulation. We, therefore, infer that the increased NGF concentration in male submaxillary glands is due to a 10-fold increase in the rate constant of synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1975.tb04416.x
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  • 7
    Electronic Resource
    Electronic Resource
    A STUDY OF THE CHANGES IN PROTEIN COMPOSITION OF MOUSE BRAIN DURING ONTOGENETIC DEVELOPMENT (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: Of the total protein in an adult mouse brain, 35 per cent is water-soluble and 65 per cent water-insoluble. Using an extraction scheme of sequential treatment with water, Triton X-100, and sodium lauryl sulphate, it was possible to solubilize at least 90 per cent of this total in distinct groups. Qualitative analysis of the extracts was achieved by electro-phoresis in porosity gradient polyacrylamide gels. In this way, each fraction was resolved into 20-50 protein bands.This sequential extraction-fractionation procedure was employed in a study of the onto-genetic changes in mouse brain proteins. The most pronounced accumulation of protein and alteration of protein composition occurred during the first few weeks after birth. Beyond that period, both quantitative and qualitative changes were much less dramatic, except in the 1 % SLS fraction, which continued to increase in size throughout the mouse's lifespan. Whereas the aqueous-soluble proteins predominated during the very early stages of development, the detergent-soluble constituents accounted subsequently for a steadily increasing proportion of the total protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb00183.x
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  • 8
    Electronic Resource
    Electronic Resource
    CHARACTERIZATION OF SULPHATIDE-CONTAINING LIPOPROTEINS IN 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: —(1) Water-soluble [35S]sulphatide is found in the 105,000 g supernatant (SN) of rat brain after intraperitoneal injection of Na235SO4. This labelled sulphatide has a density between those of free lipid and free protein.(2) Fractionation of SN by preparative acrylamide gel electrophoresis indicates that the [35S]sulphatide is not distributed among all SN proteins, but is associated with certain specific proteins. One of the isolated [35S]sulphatide-containing proteins appears homogeneous by analytical acrylamide gel electrophoresis at several pH values.(3) Comparison of the turnover of [35S]sulphatide in microsomes, SN, and myelin indicates that these three subcellular fractions behave as distinct metabolic pools, which meet the requirements for a precursor-product relationship between microsomes and SN and between SN and myelin.(4) These results suggest that sulphatide, synthesized in the microsomes, is transported to the myelin membrane as water-soluble sulphatide containing Iipoproteins in SN.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1968.tb06835.x
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  • 9
    Electronic Resource
    Electronic Resource
    Multiple forms of the nerve growth factor protein and its subunits (1968)
    s.l. : American Chemical Society
    Biochemistry 7 (1968), S. 3259-3268 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00849a032
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  • 10
    Electronic Resource
    Electronic Resource
    Developmental changes in microtubule protein of chick brain (1973)
    s.l. : American Chemical Society
    Biochemistry 12 (1973), S. 1476-1482 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00732a002
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