ArticleBiophysical journal1995
Equilibration and exchange of fluorescently labeled molecules in skinned skeletal muscle fibers visualized by confocal microscopy.
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 34 papers.
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Who cites it
34 citing papers in PubMed, 54 citations in OpenAlex.
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- AQUA Mutant Protein Quantification of Endomyocardial Biopsy-Sized Samples From a Patient With Hypertrophic Cardiomyopathy.Frontiers in cardiovascular medicine · 2022Article
- Eliminating the First Inactive State and Stabilizing the Active State of the Cardiac Regulatory System Alters Behavior in Solution and in Ordered Systems.Biochemistry · 2020Article
- ATP turnover by individual myosin molecules hints at two conformers of the myosin active site.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Diffusion coefficients of endogenous cytosolic proteins from rabbit skinned muscle fibers.Biophysical journal · 2014Article
- Definite differences between in vitro actin-myosin sliding and muscle contraction as revealed using antibodies to myosin head.PloS one · 2014Article
- Familial hypertrophic cardiomyopathy: functional variance among individual cardiomyocytes as a trigger of FHC-phenotype development.Frontiers in physiology · 2014Article
- Mechanical and kinetic properties of β-cardiac/slow skeletal muscle myosin.Journal of muscle research and cell motility · 2012Article
- ADP compartmentation analysis reveals coupling between pyruvate kinase and ATPases in heart muscle.Biophysical journal · 2010Article
- Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance.Biophysical journal · 2009Article
- Force-generating cross-bridges during ramp-shaped releases: evidence for a new structural state.Biophysical journal · 2009Article
- The mechanism of pentabromopseudilin inhibition of myosin motor activity.Nature structural & molecular biology · 2009Article
- Creatine kinase binds more firmly to the M-band of rabbit skeletal muscle myofibrils in the presence of its substrates.Molecular and cellular biochemistry · 2007Article
- Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers.Biophysical journal · 2006Article
- Initiation of the power stroke in muscle: insights from the phosphate analog AlF4.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Mechanical properties of single myosin molecules probed with the photonic force microscope.Biophysical journal · 2005Article
- Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils.The Journal of physiology · 2003Article
- Mutation of the myosin converter domain alters cross-bridge elasticity.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Confocal laser fluorescence microscopy was used to study in real time under nearly physiological conditions the equilibration and exchange characteristics of several different fluorescently labeled molecules into chemically skinned, unfixed skeletal muscle fibers of rabbit psoas. The time required for equilibration was found to vary widely from a few minutes up to several days. Specific interactions of molecules with myofibrillar structures seem to slow down equilibration significantly. Time for equilibration, therefore, cannot simply be predicted from diffusion parameters in solution. Specific interactions resulted in characteristic labeling patterns for molecules like creatine kinase (muscle type), pyruvate kinase, actin-binding IgG, and others. For the very slowly equilibrating Rh-NEM-S1, changes in affinity upon binding to actin in the absence of calcium and subsequent slow cooperative activation, beginning at the free end of the filament at the H-zone, were observed. In the presence of calcium, however, binding of Rh-NEM-S1 was homogeneous along the whole actin filament from the very beginning of equilibration. The dissociation properties of the dynamic interactions were analyzed using a chase protocol. Even molecules that bind with rather high affinity and that can be removed only by applying extreme experimental conditions like Rh-phalloidine or Rh-troponin could be displaced easily by unlabeled homologous molecules.
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