ArticleBiophysical journal1995
BDM compared with P(i) and low Ca2+ in the cross-bridge reaction initiated by flash photolysis of caged ATP.
Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 13 citations in OpenAlex.
- Tetrahydrobiopterin improves diastolic dysfunction by reversing changes in myofilament properties.Journal of molecular and cellular cardiology · 2013Article
- Effect of inorganic phosphate on the force and number of myosin cross-bridges during the isometric contraction of permeabilized muscle fibers from rabbit psoas.Biophysical journal · 2008Article
- Molecular basis of the catch state in molluscan smooth muscles: a catchy challenge.Journal of muscle research and cell motility · 2008Review
- ATP utilization for calcium uptake and force production in different types of human skeletal muscle fibres.The Journal of physiology · 2001Article
- Single turnover of cross-bridge ATPase in rat muscle fibers studied by photolysis of caged ATP.Journal of muscle research and cell motility · 2001Article
- Effects of ADP and low ATP on the Ca(2+)-sensitive transient contraction upon photolysis of caged ATP in rat muscle fibres: a study on the Bremel-Weber type cooperation.Journal of muscle research and cell motility · 1998Article
- Mechanical study of rat soleus muscle using caged ATP and X-ray diffraction: high ADP affinity of slow cross-bridges.The Journal of physiology · 1997Article
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3 authors at 1 institution in 1 country.
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Abstract
Using flash photolysis of caged ATP in skinned muscle fibers from rat psoas, we examined the inhibitory effects of 2,3-butanedione monoxime (BDM) on the contraction kinetics and the rate of ATP hydrolysis of the cross-bridges at approximately 10 degrees C. The hydrolysis rate was estimated from the stiffness records. The effects of BDM were compared with those of orthophosphate (P(i)) and of reduction in [Ca2+] (low Ca2+), and it was found that i) BDM and low Ca2+ inhibited ATPase activity to the same extent as they inhibited the steady tension, whereas P(i) inhibited ATPase activity much less than tension; ii) BDM and P(i) decreased tension per stiffness during the steady contraction more than did low Ca2+; iii) neither BDM nor low Ca2+ affected the initial relaxation of the fiber on release of ATP, but P(i) slightly slowed it; and iv) BDM hardly influenced the rate of contraction development after relaxation, although P(i) and low Ca2+ accelerated it. We concluded that BDM inhibits the Ca(2+)-regulated attachment of the cross-bridges and force-generation of the attached cross-bridges.
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