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The secondary structure of myelin basic protein extracted by deoxycholate.
Biochimica Et Biophysica Acta
|April 25, 1977
Summary
Myelin basic protein (MBP) structure is influenced by extraction methods. Deoxycholate extraction reveals a more helical MBP structure compared to conventional methods, suggesting its in vivo conformation may be more ordered.
Area of Science:
- Neuroscience
- Biochemistry
- Structural Biology
Background:
- Myelin basic protein (MBP) is implicated in neurological diseases.
- The in vivo structure of MBP is of significant interest due to its role in disease.
- Conventional extraction methods using organic solvents may alter MBP structure.
Purpose of the Study:
- To investigate the influence of extraction methods on MBP secondary structure.
- To determine if deoxycholate extraction preserves MBP's native conformation.
- To compare the structure of deoxycholate-extracted MBP with conventionally prepared MBP.
Main Methods:
- Extraction of MBP from bovine myelin using deoxycholate.
- Purification of MBP using gel chromatography.
- Secondary structure analysis via circular dichroism spectroscopy.
Main Results:
- Deoxycholate-extracted MBP exhibited 8-14% more helical structure than chloroform/methanol-extracted MBP.
- This increased helical content was observed in both acetate and Tris buffers.
- The conformational change was independent of NaCl concentration.
Conclusions:
- Deoxycholate extraction may yield an MBP structure closer to its in vivo conformation.
- MBP might adopt a more ordered, helical structure within the myelin sheath.
- The refolding ability of MBP may explain its retained encephalitogenic activity after harsh treatments.