Isolation and partial characterization of the major proteins of rabbit sciatic nerve myelin

Brostoff, Steven W.; Karkhanis, Yashwant D.; Carlo, Dennis J.; Reuter, W.; Eylar, E.H.

doi:10.1016/0006-8993(75)90895-1

Cited by 94 publications

(25 citation statements)

References 18 publications

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“…A unique basic protein, BF-P2, was observed in PNS myelin in addition t o the BP which is common t o myelin of b o t h the CNS a n d PNS (UYEMURA et a/., 1970;BROSTOFF & EYLAR, 1972;BROSTOFF et al, 1974;KITAMURA et al, 1975). Next, t w o glycoproteins, BR-PO (EVERLY et WOOD & DAWSON, 1973;SINGH & SPRITZ, 1974;BROSTOFF et a!., 1975;KITAMURA et a/., 1976) and PASII (KITAMURA et a/., 1976;UYEMURA et a!., 19776, 1978), b o t h of which are unique to PNS myelin, were found t o be commonly localized in the PNS myelin of mammalian species. We have previously described the purification and characterization of these basic proteins and glycoproteins from PNS myelin (UYE-MURA et a/., 1970, 1972, 1977a, 6, 1978KITAMURA et a/., 1975KITAMURA et a/., , 1976.…”

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confidence: 98%

Developmental Changes of Myelin Proteins in the Chick Peripheral Nerve

Uyemura

Horie

Kïtamura

et al. 1979

Journal of Neurochemistry

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Abstract— Developmental changes of myelin proteins in chick sciatic nerve were studied at the stage of myelination by sodium dodecylsulfate (SDS)‐polyacrylamide gel electrophoresis. The myelin of adult hen peripheral nervous system (PNS) contained two glycoproteins (BR‐P0 and PASII), both of which are unique to PNS myelin, in addition to the basic encephalitogenic protein, BP, which is common to CNS and PNS myelin. The other basic protein (BF‐P2) found in the PNS of other species was not definitely detectable in hen PNS. At the early stages of myelination (from 14 to 18 embryonic days) the amounts of myelin proteins increased rapidly in parallel with the increase in number of layers of the myelin sheath of the PNS. At 14 embryonic days high molecular weight proteins were dominant, while myelin specific proteins were barely detectable in the PNS myelin fraction. At 18 embryonic days, however, BR‐PO, BP and PASII proteins became the main protein components of the PNS myelin, whereas high molecular weight proteins decreased in quantitative importance during development. At the early stage of myelination other glycoproteins were also detectable in the PNS myelin. Radioactive fucose was actively incorporated into the two glycoproteins, BR‐P0 and PASII, at the early stage of myelination in vivo. These results suggested that myelin proteins especially glycoproteins, may play an important role in PNS myelin formation.

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mentioning

confidence: 98%

Developmental Changes of Myelin Proteins in the Chick Peripheral Nerve

Uyemura

Horie

Kïtamura

et al. 1979

Journal of Neurochemistry

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“…Like its CNS counterpart, it is methylated and phosphorylated (Wiggins and Morell, 1980) and can act as an acceptor for N-acetylgalactosamine . The CNS and PNS proteins appear to be the same in all aspects studied thus far (Brostoff et al, 1975b), including physiochemical measurements, peptide maps, and immunological properties (see Chapter 12).…”

Section: B Pi Basic Proteinmentioning

confidence: 98%

“…Both Y and X can be fucosylated in vitra . By analogy to CNS tissue, PNS MBPs, (both PI and Pz) can be recovered from homogenates of PNS nerve tissue by acid extraction after delipidation and can be further purified by gel filtration or ion-exchange chromalOgraphy or both (Brostoff et al, , 1975bKitamura et al, 1975). The solubility properties of iso la ted PNS myelin, however, differ considerably from those of CNS myelin.…”

Section: Peripheral Nervous Systemmentioning

confidence: 99%

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Myelin

1984

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“…All of the procedures involve solubilization of the residue remaining after removal of basic proteins (PI and P2) by acid extraction and delipidation with organic solvents. The residue from these treatments was solubilized with phenol-acetic acid-water (Brostoff et al, 1975) or sodium dodecyl sulfate (Kitamura et al, 1976;Roomi et al, 1978). Proteins were then purified by gel filtration in the presence of detergent on an appropriate column.…”

Section: Purification and Characterization Of Specific Glycoproteinsmentioning

confidence: 99%