[Interaction of the enzymes of cellular energy support with the F-actin of the thin filaments of muscle fiber. I. The binding of lactate dehydrogenase with F-actin induces changes in the structural state of the components of the complex].
A study was made of changes in F-actin conformation occurring in a myosin-free single ghost fibre induced by the binding of glycolytic enzyme lactate dehydrogenase (LDG) to F-actin. The formation of the complex between LDG and F-actin induces changes in the parameters of the intrinsic (tryptophan) and extrinsic (rodominil--phalloin) polarized fluorescence of F-actin of the ghost muscle fibre. It is found that LDG stimulates Mg2+-ATPase of actomyosin in solution. It is assumed that the coupling of energy-providing mechanism with that of muscle contraction may be accomplished through the conformation changes in F-actin.
Kirillina
V P
VP
Stabrovskaia
V I
VI
Borovikov
Iu S
IuS
D000199:Actins / Q000378:metabolism*; D000205:Actomyosin / Q000378:metabolism; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D004734:Energy Metabolism; D006019:Glycolysis; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D008859:Microscopy, Polarization; D009132:Muscles / Q000201:enzymology* / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D000205:Actomyosin; D007770:L-Lactate Dehydrogenase; D017301:Ca(2+) Mg(2+)-ATPase
Vzaimodeĭstvie fermentov énergoobespecheniia kletki s F-aktinom tonkikh niteĭ myshechnogo volokna. I. Sviazyvanie laktatdegidrogenazy s F-aktinom indutsiruet izmeneniia strukturnogo sostoianiia komponentov kompleksa.