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[Spectroscopic study of myosin from denervated rabbit muscles]
Abstract:
Spectra of tryptophan UV-fluorescence and UV-absorption of myosin isolated 30 days after denervation of white skeletal muscles of rabbit were studied. It has been observed that fluorescence intensity of such myosin in the maximum decreases. This decrease becomes more pronounced after purification of protein from admixtures. It has been shown that after denervation the absorption at 260 nm increases, however, the difference disappears after myosin purification. The data obtained point to a change of myosin structural state after denervation.
Insights
Denervation of rabbit white skeletal muscles alters myosin structure. Tryptophan fluorescence intensity decreases, and UV absorption at 260 nm increases, indicating changes in protein state.
Area of Science:
- Biochemistry
- Molecular Biology
- Muscle Physiology
Context:
- Skeletal muscle denervation leads to significant physiological and molecular changes.
- Myosin, a key contractile protein, is susceptible to alterations following nerve damage.
Purpose:
- To investigate the effects of denervation on the spectral properties of myosin.
- To analyze changes in tryptophan UV-fluorescence and UV-absorption of myosin.
Summary:
- Myosin was isolated from rabbit white skeletal muscles 30 days post-denervation.
- A decrease in maximum fluorescence intensity and an increase in UV absorption at 260 nm were observed.
- These spectral changes were more pronounced after protein purification, suggesting intrinsic alterations in myosin.
Impact:
- The findings indicate a change in the structural state of myosin following denervation.
- This research contributes to understanding the molecular mechanisms of muscle atrophy and protein remodeling.