Gene/Protein
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Enzyme
Compound
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Gene/Protein
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Target Concepts:
Gene/Protein
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Query: EC:3.6.3.1 (
Mg2+-ATPase
)
1,484
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The changes in conformation of F-actin induced by the binding of the
glycolytic enzyme
lactate dehydrogenase were studied in myosin-free single ghost muscle fibres. The formation of the lactate dehydrogenase-F-actin complex was accompanied by changes in the parameters of intrinsic (tryptophan) and extrinsic (rhodaminyl-phalloin) polarized fluorescence of ghost muscle fibre F-actin. Lactate dehydrogenase stimulated actin-activated
Mg2+-ATPase
of myosin subfragment 1 by 30%. F-actin of ghost fibres depressed lactate dehydrogenase activity to 20% of the initial values. It is suggested that the energy-providing mechanism is coupled with that of muscle contraction through conformational changes in F-actin.
...
PMID:Lactate dehydrogenase-induced conformational changes of F-actin in myosin-free ghost single fibres. 253 93
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.
...
PMID:[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]. 297 67