[Effect of the innervation on the structural state of F-actin in rat fast muscles].
Effect of denervation and damage of the spinal cord on the structural state of F-actin in muscle extensor digitorum longus of a rat was studied by polarized microfluorimetry in the ultraviolet light region. The ability of F-actin to change its conformation at ATP binding was used as a test. The character of the changes in tryptophan polarized fluorescence induced by ATP binding was different at muscle denervation and at the damage of the spinal cord. A suggestion is made that the structural state of F-action in muscle fibres may depend on muscle innervation.
Borovikov
Iu S
IuS
Carlson
B M
BM
Aksenova
N B
NB
Loubert
P
P
D000199:Actins / Q000378:metabolism / Q000648:ultrastructure*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D003592:Cytophotometry; D003655:Decerebrate State / Q000378:metabolism / Q000473:pathology; D005454:Fluorescence Polarization; D009121:Muscle Denervation; D009132:Muscles / Q000294:innervation* / Q000378:metabolism / Q000637:transplantation / Q000648:ultrastructure; D011487:Protein Conformation; D051381:Rats; D011916:Rats, Inbred F344
D000199:Actins; D000255:Adenosine Triphosphate
Vliianie innervatsii na strukturnoe sostoianie F-aktina v bystrykh myshtsakh krysy.