1986
DOI: 10.1016/s0300-9084(86)80161-4
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Purification and characterization of minor brain proteolipids: use of fast atom bombardment — mass spectrometry for peptide sequencing

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Cited by 24 publications
(18 citation statements)
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“…The high molecular weight form represents aggregated forms of PLP (Chan and Lees, 1974), and the lower molecular weight form appears to have similar sequence to the major myelin proteolipid forms (Lepage et al, 1986). The brain lysate preparation showed two bands at the 16 and 14 kD, two forms that were previously described (Lepage et al, 1986). In the extracts from immune cells 2 major bands were evident, the high and low molecular weight (16 and 50 kD), but there was no band of 25 kD.…”
Section: Western Blotting With Anti-plp Antibodiesmentioning
confidence: 64%
See 1 more Smart Citation
“…The high molecular weight form represents aggregated forms of PLP (Chan and Lees, 1974), and the lower molecular weight form appears to have similar sequence to the major myelin proteolipid forms (Lepage et al, 1986). The brain lysate preparation showed two bands at the 16 and 14 kD, two forms that were previously described (Lepage et al, 1986). In the extracts from immune cells 2 major bands were evident, the high and low molecular weight (16 and 50 kD), but there was no band of 25 kD.…”
Section: Western Blotting With Anti-plp Antibodiesmentioning
confidence: 64%
“…With the commercial antibody AHP261, the myelin preparation showed 4 major bands in the regions of 7, 16, 25, and 50 kD. The high molecular weight form represents aggregated forms of PLP (Chan and Lees, 1974), and the lower molecular weight form appears to have similar sequence to the major myelin proteolipid forms (Lepage et al, 1986). The brain lysate preparation showed two bands at the 16 and 14 kD, two forms that were previously described (Lepage et al, 1986).…”
Section: Western Blotting With Anti-plp Antibodiesmentioning
confidence: 69%
“…an isoform of PLP generated by alternative splic ing in exon 3 [14]. Lepage et al [15], later confirmed by Schindler el al. [16], found minor proteolipids in the mammalian CNS.…”
Section: Alternative Splicing Of Plpmentioning
confidence: 89%
“…In the rat cultures a low molecular weight (approximately 14 kD) PLP immunoreactive protein was observed, following the same developmental course as the PLP protein which was not detected in mouse OL. These bands likely represent the low molecular weight species of proteolipid protein that is related to the major PLP reported by Lepage et al [17]. From these data it was not possible to determine if the 14-kD protein is absent from mouse OL or simply below the detection limits of this assay.…”
Section: Developmental Expression Of Myelin Proteins In Enriched Mousmentioning
confidence: 82%
“…Monitoring the num ber of OL in the mixed glial cultures during development revealed that the rat cultures contained approximately five-fold more OL than the mouse cultures, and this ratio remained constant throughout development [8,13], Even taking this difference into consideration, the number of developing OL in the enriched mouse cultures was still less than anticipated. This could indicate that mouse OL require a longer period of maturation in primary culture before they can be successfully subcultured [17] and/or that more of the mouse OL are in a bipotential stage (O-2A or 0 4) during the isolation protocol and upon replat ing in serum-containing media redifferentiate into astro cytes [16], This theory may get some support from the greater response of the enriched mouse cultures to treat ment with PDGF/FGF. Wolswijk et al [27J report the PDGF is a potent mitotic factor for 0-2A adul1 progenitor cells, and upon the addition of PDGF along with FGF to our cultures, a 25% increase in the number of GC-posi- 78 Ducliala/Asolra/Macklin Cell Surface Markers and Myelin Proteins in Cultured Oligodendrocytes tive cells in enriched mouse cultures was noted, whereas the comparable rat cultures only exhibited a 15% increase.…”
Section: Discussionmentioning
confidence: 99%