Salt-soluble myelin basic protein is degraded by myelin-adsorbed proteinases
Myelin basic protein (MBP) is partially released from isolated myelin membranes by high ionic strength (1). Extracts contain traces of endoproteinases, as evident from the limited proteolysis of MBP of extracts on incubation (2,3). The exact origin of these pro-teinases has remained equivocal (4). W...
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| Main Authors: | , |
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| Format: | Chapter/Article Conference Paper |
| Language: | English |
| Published: |
1997
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| In: |
Neurochemistry
Year: 1997, Pages: 1111-1115 |
| DOI: | 10.1007/978-1-4615-5405-9_187 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/978-1-4615-5405-9_187
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| Author Notes: | U. Haas and H.H. Berlet |
| Summary: | Myelin basic protein (MBP) is partially released from isolated myelin membranes by high ionic strength (1). Extracts contain traces of endoproteinases, as evident from the limited proteolysis of MBP of extracts on incubation (2,3). The exact origin of these pro-teinases has remained equivocal (4). We now present evidence in support of apparent extrinsic proteinase activities of myelin being loosely adsorbed onto myelin surfaces. They were found to be soluble in Tris buffer of low ionic strength along with a number of as yet unidentified proteins. The implications of this observation on the in vitro proteolysis of salt-soluble MBP were examined. |
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| Item Description: | Gesehen am 26.03.2024 |
| Physical Description: | Online Resource |
| ISBN: | 9781461554059 |
| DOI: | 10.1007/978-1-4615-5405-9_187 |