title: Regulatory light chain influences alterations of myosin head induced by actin.
abstract: The effect of magnesium-for-calcium exchange and phosphorylation of regulatory light chain (LC2) on structural organization of rabbit skeletal myosin head was studied by limited tryptic digestion. In the presence of actin, exchange of magnesium bound to LC2 by calcium in dephosphorylated myosin accelerates the digestion of myosin and heavy meromyosin heavy chain and increases the accumulation of a 50 kDa fragment. This effect is significantly diminished in the case of phosphorylated myosin. Thus, both phosphorylation and cation exchange influences the effect of actin binding on the structural organization of myosin head.
authors.affiliation: Research Institute of Physiology, Kiev State University, USSR.
authors.forename: E B
authors.initials: EB
authors.lastname: Babiychuk
authors.forename: D
authors.initials: D
authors.lastname: Stepkowski
authors.forename: V M
authors.initials: VM
authors.lastname: Danilova
authors.forename: I
authors.initials: I
authors.lastname: Kakol
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D002918:Chymotrypsin / Q000378:metabolism; D007700:Kinetics; D009132:Muscles / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification; D010748:Phosphopeptides / Q000302:isolation & purification; D010766:Phosphorylation; D011817:Rabbits; D014357:Trypsin / Q000378:metabolism
chemical_list: D000199:Actins; D010446:Peptide Fragments; D010748:Phosphopeptides; D002918:Chymotrypsin; D014357:Trypsin; D009218:Myosins