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J. Matthieu, A. Zimmerman, H. Webster, A. Ulsamer, R. Brady, R. Quarles (1974)
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STUDIES ON THE MECHANISM OF DEMYELINATION: TRIETHYL TIN‐INDUCED DEMYELINATIONJournal of Neurochemistry, 21
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(1975)
Myelin autolysis in edema
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MYELIN BASIC PROTEIN IN FROZEN AND UNFROZEN BOVINE BRAIN: A STUDY OF AUTOLYTIC CHANGES IN SITU 1Journal of Neurochemistry, 25
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Localization of Encephalitogenic Basic Protein in the Intraperiod Line of Lamellar MyelinNature, 227
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AN IN VITRO SYSTEM FOR THE STUDY OF MYELIN SYNTHESIS 1Journal of Neurochemistry, 16
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CHARACTERIZATION AND PROTEIN ANALYSIS OF MYELIN SUBFRACTIONS IN RAT BRAIN: DEVELOPMENTAL AND REGIONAL COMPARISONSJournal of Neurochemistry, 25
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Myelin breakdown and basic protein.Experimental neurology, 45 1
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K. Weber, M. Osborn (1969)
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.The Journal of biological chemistry, 244 16
Marion Smith, L. Sedgewick, J. Tagg (1974)
PROTEOLYTIC ENZYMES AND EXPERIMENTAL DEMYELINATION IN THE RAT AND MONKEYJournal of Neurochemistry, 23
G. Buletza, M. Smith (1976)
Enzymic hydrolysis of myelin basic protein and other proteins in central nervous system and lymphoid tissues from normal and demyelinating rats.The Biochemical journal, 156 3
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M. Canto, H. Wiśniewski, Anne Johnson, S. Brostoff, C. Raine (1975)
Vesicular disruption of myelin in autoimmune demyelinationJournal of the Neurological Sciences, 24
Abstract— The effects on myelin of autolysis in situ after death and after purification were studied in normal brains and spinal cords and in those made edematous as a result of chronic triethyl tin (TET) feeding. Myelin prepared from normal and edematous brains and spinal cords autolyzed for 12 h at 4°C contained only slightly less basic protein than that prepared from freshly killed animals. The amounts of a light lipid‐protein fraction (dissociated myelin) usually obtained during purification of myelin from edematous CNS were about the same in tissue from freshly killed rats and those autolyzed for 12 h at 4°C. Autolysis for 12 h at room temperature resulted in formation of large amounts of dissociated myelin and loss of basic protein, but more dissociation and basic protein loss occurred in CNS from edematous brains and spinal cords than from the normal. Purified myelin prepared from freshly‐killed normal and TET‐fed rats was incubated at 37°C in media of several ionic strengths. In Krebs‐Ringer bicarbonate (physiological extracellular fluid) extensive dissociation of myelin occurred with much less in 0.04 M‐Tris buffer, pH 7.2, and only small amounts were formed in 0.01 M‐Tris. In all cases myelin from edematous CNS formed more dissociated fraction than did the normal myelin. Basic protein loss was also proportional to the ionic strength of the media, but there was no difference in loss between normal and TET‐myelin. Two different factors, proteolysis and physical extraction of basic protein by salt solutions, may be contributing to myelin dissociation and loss of basic protein.
Journal of Neurochemistry – Wiley
Published: Feb 1, 1977
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