title: Is there any difference between actins from intact and denervated muscles?
abstract: Various techniques have been used (UV absorbance and fluorescence spectroscopy, polarised UV fluorescence microscopy, viscosimetry, electrophoresis and isoelectric focusing, superprecipitation, etc.) As suggested by several parameters, denervation interferes with the structure of actin by producing local conformation changes in the region of aromatic residues near the sites responsible for actin-actin and actin-myosin interactions.
mesh_terms: D000199:Actins / Q000302:isolation & purification*; D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D011232:Chemical Precipitation; D004586:Electrophoresis; D005454:Fluorescence Polarization; D007525:Isoelectric Focusing; D009121:Muscle Denervation; D009132:Muscles / Q000032:analysis*; D011487:Protein Conformation; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000199:Actins; D000251:Adenosine Triphosphatases