The effect of denervation upon the functional properties of myosin and its fragments.
A study has been made of some structural and enzymatic properties of myosin and its fragments from denervated white muscles of rabbit in the course of atrophy using different methods: UV-luminiscence, flow birefringence, electromicroscopy, viscosimetry and enzymatic measurements. All the studied parameters had a tendency to decrease; at prolonged observation some properties were partially restored. Considerable changes of structural properties of LMM were revealed: the ability of LMM from denervated muscle to form high-ordered structures which is characteristic of LMM from normal muscle decreased considerably.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001718:Birefringence; D002802:Cholinesterases / Q000378:metabolism; D008163:Luminescent Measurements; D008854:Microscopy, Electron; D009121:Muscle Denervation; D009218:Myosins / Q000378:metabolism; D011487:Protein Conformation; D011817:Rabbits; D013057:Spectrum Analysis; D013997:Time Factors; D014783:Viscosity
D002802:Cholinesterases; D000251:Adenosine Triphosphatases; D009218:Myosins