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  • 1970-1974  (14)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN—XII ANIONIC STAINING OF MYELIN BASIC PROTEINS FOR HISTOLOGY, ELECTROPHORESIS AND ELECTRON MICROSCOPY (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: Abstract— Phosphotungstic acid haematoxylin, trypan blue and amidoblack techniques have been developed as anionic dye methods for staining myelin basic proteins. All methods displayed central and peripheral nervous system myelin in histochemical prepa rations and stained brain basic proteins in electrophoretic polyacrylamide gels: phosphotungstic acid haematoxylin appeared to be the most selective of these techniques. Electron photomicrographs of peripheral nerve stained by phosphotungstic acid haematoxylin showed that the major part of myelin basic protein is located in the period dense line. The basic proteins stained by phosphotungstic acid haematoxylin showed an early loss in rat sciatic nerve undergoing Wallerian degeneration and had completely disappeared from the centre of 20 plaques of multiple sclerosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb11966.x
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  • 2
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN. XIII DIGESTION OF BASIC PROTEIN OUTSIDE ACUTE PLAQUES OF MULTIPLE SCLEROSIS (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: Abstract— Plaques of multiple sclerosis from a patient with a short clinical history were investigated by qualitative and quantitative histochemical methods. One of three plaques examined showed perivenous lymphocytic infiltration; this plaque was regarded as a particularly early acute lesion. In this plaque a relatively wide zone of diminished staining for basic protein extended outwards around the edge of the lesion. A narrower and irregular zone of diminished cerebroside staining was also seen around the plaque. Staining for phosphoglycerides and cholesterol was relatively normal up to the edge of the lesion; no zone of reduced staining for these lipids was seen outside the plaque. Proteolytic activity was increased throughout the lesion (pH 3.5 〉 7.4). The two less acute plaques showed no obvious loss of basic protein and cerebroside outside the plaque. Addendum: Two further acute plaques of multiple sclerosis obtained recently, showed a similar loss of basic protein outside of lesion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb00010.x
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  • 3
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN–XV. CHANGES IN THE MYELIN PROTEINS OF THE PERIPHERAL NERVE UNDERGOING WALLERIAN DEGENERATION–ELECTROPHORETIC AND MICRODENSITOMETRIC OBSERVATIONS (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 chronological order of changes in rat peripheral nerve proteins during Wallerian degeneration has been investigated by microdensitometric and electrophoretic techniques. Both methods revealed an early loss of myelin proteins. The histochemical microdensitometric study showed a very substantial early loss of stainable protein basic groups and a somewhat slower progressive loss of the major protein component of peripheral nerve myelin (the J band). The electrophoretic study showed an early loss of both the J band protein and the slower-moving basic protein band. The histochemical study also suggested that some cerebroside may be lost in the early stage of Wallerian degeneration. It is concluded that degradation of myelin proteins is an initial event in the process of myelin breakdown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb05114.x
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  • 4
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN XIV PERIPHERAL NERVE MYELIN PROTEINS: ELECTROPHORETIC AND HISTOCHEMICAL CORRELATIONS (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— Myelin from the peripheral nervous system has been shown to contain two basic protein components and an electrophoretically slower-moving major protein, the ‘J’ band. The ‘J’ band protein cannot be selectively removed by aqueous or organic solvents and does not correspond to proteolipid or acidic protein. Histochemical stains applied to peripheral nervous systems myelin proteins separated by polyacrylamide electrophoresis indicate that ‘J’ band protein is analogous with the neurokeratin of the nerve sheath. Trypanophilia observed histochemically in unfixed myelin is principally due to basic proteins. With prolonged tryptic digestion ‘J’ band protein is degraded. Thus, previous classifications of myelin proteins based on trypsin sensitivity have been modified. All peripheral nervous system myelin proteins should be regarded as trypsin-sensitive, the basic protein being relatively more and the ‘J’ band protein relatively less susceptible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01481.x
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  • 5
    Electronic Resource
    Electronic Resource
    PROTEOLYTIC ACTIVITY AND BASIC PROTEIN LOSS IN AND AROUND MULTIPLE SCLEROSIS PLAQUES: COMBINED BIOCHEMICAL AND EIISTOCHEMICAL OBSERVATIONS (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— This combined histochemical and biochemical study has shown that acid proteinase activity (PH 3.5) is increased around histologically-defined active plaques of multiple sclerosis (MS). Biochemical estimation showed that the enzyme is more active in most samples of ‘normal’ white matter in MS than in controls. A gradient of enzyme activity was observed: control white matter-white matter distant from plaqueclose white matter-edgsplaque. Both electrophoretic and histochemical techniques revealed a reduction or absence of basic (encephalitogenic) protein in the plaques. Electrophoresis showed a diminution of encephalitogenic protein outside some plaques. Phospholipids that remain on the base-line of thin-layer chromatoplates were shown to be predominantly phosphoinositides combined with encephalitogenic protein
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01382.x
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  • 6
    Electronic Resource
    Electronic Resource
    Biological Sciences: Cellular Lipid Inclusions in the White Matter in Multiple Sclerosis (1971)
    [s.l.] : Nature Publishing Group
    Nature 233 (1971), S. 264-265 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Seventeen plaques from eight cases of multiple sclerosis and white matter from sixteen control patients, who had died from other neurological diseases, were fixed in routine saline-formol and transferred to 1% calcium acetate?10% formalin. Frozen sections were stained with haematoxylin-eosin, Sudan ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/233264a0
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  • 7
    Electronic Resource
    Electronic Resource
    Schiff reactions with lipids and the disputed terminal rinse with hydrochloric acid (1971)
    Springer
    Histochemistry and cell biology 28 (1971), S. 220-224 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary We have been concerned with the effect of 3N HCl on the reaction-products of lipids and Schiff's reagent in the PAS and plasmal reactions. Our conclusions are: 1. We agree with Elleder and Lojda (1971) that the intensity of the modified PAS and plasmal reactions is reduced if a terminal 3N HCl rinse is used. However, we consider that the term “rinse” is not synonomous with a 5–10 min wash or bath. 2. We do not agree that this reduction is substantial. After a 1 min rinse with 3N HCl, it amounts to only 9.1% with the plasmal and 25.4% with the modified PAS reaction. 3. We do not agree that this modest reduction is necessarily all due to the release of fatty (or glycollic) aldehydes from conjugation with Schiff's reagent; it could equally well be due to suppression of phospholipid (or other anion) staining by the residual basic fuchsin in Schiff's reagent. 4. We do not agree that the plasmal (or PAS) reaction of brain lipids on paper is nearly extinguished by a terminal rinse in 3N HCl: such a result is possibly due to imperfect washing of chromatograms. With a terminal rinse of 1 min, the reactions were reduced by 31.5% and nil, respectively. 5. We do not agree that “the influence of an acid mounting medium” is of any practical significance with these histochemical reactions. 6. Finally we wish to reiterate that the staining of phospholipids (or other anions) by the residual basic fuchsin in Schiff's reagent is potentially a very real hazard in the application of the modified PAS and plasmal methods. Our experiments suggest that this hazard can be obviated by the use of the brief terminal 3N HCl rinse. Even if the acid does remove part of the reaction product with some Schiff methods, it is perhaps safer on these occasions to lose some of the baby with the bath-water.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305676
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  • 8
    Electronic Resource
    Electronic Resource
    Comment on the note by Z. Lojda and M. Elleder (1971)
    Springer
    Histochemistry and cell biology 28 (1971), S. 229-230 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305678
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  • 9
    Electronic Resource
    Electronic Resource
    Histochemistry of myelin. IX. Neutral and acid proteinases in early Wallerian degeneration (1970)
    Springer
    Journal of molecular histology 2 (1970), S. 209-218 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Acid and neutral proteinases, ‘leucine aminopeptidase’ (l-leucyl-β-naphthylamidase) and acid phosphatase were studied in rat sciatic nerves undergoing Wallerian degeneration. Biochemical evidence indicated that increased activity of both proteases and acid phosphatase occurred by 12 hr after nerve section. Histochemical changes in these three enzymes were apparent after three days. Biochemical estimation of neutral ‘leucine aminopeptidase’ (an enzyme predominantly located in myelin in the normal peripheral nerve) showed increased activity near the of the first week of degeneration. During the second week after nerve section all the enzymes studied became markedly more active. The parallel increase in activity of acid proteinase and acid phosphatase and the similarities in their histochemical distribution suggest that the acid proteinase is of lysosomal origin. Such changes in early Wallerian degeneration appear to precede macrophage invasion of the nerve and to arise mainly from the degenerating axon, the Schwann cell, or both. In spite of the delayed increase in ‘leucine aminopeptidase’ it seems possible that some proteinase activity also arises from myelin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003470
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  • 10
    Electronic Resource
    Electronic Resource
    Bromine-Sudan Black: a general stain for lipids including free cholesterol (1972)
    Springer
    Journal of molecular histology 4 (1972), S. 505-515 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Preliminary bromination (with bromine water) increases the intensity of staining of tissue lipids with Sudan Black and certain other dyes. The mechanism appears to be due to the formation of sudanophilic bromo-derivatives of cholesterol and to the retention of certain other lipids, notably phosphatidyl choline and free fatty acids, during staining. The advantage of the bromine-Sudan Black method is that all tissue lipids are stained, except saturated fatty acids, saturated triglycerides and perhaps saturated cholesterol esters. In practice, such lipids rarely, if ever, occur alone, and normally are admixed with their stainable unsaturated counterparts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01011130
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