A biochemical comparison ofXenopus laevis and mammalian myelin from the central and peripheral nervous systems
| Autor: | J. L. Everly, H.deF. Webster, Richard H. Quarles, Bruce D. Trapp, C. F. Pasnak, N. Sakuragawa |
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| Rok vydání: | 1978 |
| Předmět: |
Proteolipid protein 1
Central nervous system Xenopus Membrane Lipids Cellular and Molecular Neuroscience chemistry.chemical_compound Myelin Mole medicine Animals Sodium dodecyl sulfate Myelin Sheath Glycoproteins Brain Chemistry chemistry.chemical_classification biology urogenital system General Neuroscience biology.organism_classification Sciatic Nerve Rats Cell biology Molecular Weight medicine.anatomical_structure Spinal Cord nervous system chemistry Immunology Sciatic nerve 2' 3'-Cyclic-Nucleotide Phosphodiesterases Glycoprotein Myelin Proteins |
| Zdroj: | Journal of Neurobiology. 9:217-228 |
| ISSN: | 1097-4695 0022-3034 |
| DOI: | 10.1002/neu.480090304 |
| Popis: | Myelin purified from the central nervous system of Xenopus laevis contained the same major lipid and protein components as human myelin. However, some minor differences in the myelin proteins were noted. The Xenopus basic protein had a higher apparent mol wt. on sodium dodecyl sulfate gels than the corresponding mammalian protein. The absolute specific activity of 2',3'-cyclic nucleotide 3'-phosphohydrolase in the Xenopus myelin was considerably higher than in mammals. There were differences in the high mol wt. proteins, and the glycoproteins in Xenopus myelin were more heterogeneous than those in mammals. Peripheral myelin from Xenopus sciatic nerve was compared with that from the rat. The lipids in the two types of myelin were similar. There was a major glycoprotein in the Xenopus myelin corresponding to the P0 protein and a basic protein of slightly larger mol wt. than the P1 protein of rat myelin. |
| Databáze: | OpenAIRE |
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