Topology of wolfgram proteins and 2?, 3?-cyclic nucleotide 3?-phosphodiesterase in CNS myelin: Studies with proteases
| Autor: | K. V. Raja Rao, P. S. Sastry, Geeta S. Vemuri |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1994 |
| Předmět: |
Central Nervous System
Lipid Bilayers Biology Topology Aminopeptidase Biochemistry 2' 3'-Cyclic-nucleotide 3'-phosphodiesterase Cellular and Molecular Neuroscience Myelin Western blot Thermolysin Endopeptidases medicine Animals Humans Myelin Sheath medicine.diagnostic_test Phosphodiesterase General Medicine Trypsin Molecular biology medicine.anatomical_structure Myelinogenesis 2' 3'-Cyclic-Nucleotide Phosphodiesterases Myelin Proteins medicine.drug |
| Zdroj: | IndraStra Global. |
| ISSN: | 2381-3652 |
| Popis: | The topological disposition of Wolfgram proteins (WP) and their relationship with 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) in human, rat, sheep, bovine, guinea pig and chicken CNS myelin was investigated. Controlled digestion of myelin with trypsin gave a 35KDa protein band (WP-t) when electrophoresed on dodecyl sulfate-polyacrylamide gel in all species. Western blot analysis showed that the WP-t was derived from WP. WP-t was also formed when rat myelin was treated with other proteases such as kallikrein, thermolysin and leucine aminopeptidase. Staining for CNPase activity on nitrocellulose blots showed that WP-t is enzymatically active. Much of the CNPase activity remained with the membrane fraction even after treatment with high concentrations of trypsin when WP were completely hydrolysed and no protein bands with M.W > 14KDa were detected on the gels. Therefore protein fragments of WP with M.W < 14KDa may contain CNPase activity. From these results, it is suggested that the topological disposition of all the various WP is such that a 35KDa fragment is embedded in the lipid bilayer and the remaining fragment exposed at the intraperiod line in the myelin structure which may play a role in the initiation of myelinogenesis. |
| Databáze: | OpenAIRE |
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