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Neonatal And Adult Myosin Heavy Chains Form Homodimers During ... - Jcb Rupress
Get Neonatal And Adult Myosin Heavy Chains Form Homodimers During ... - Jcb Rupress
Everett Bandman* * Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254; and Department of Food Service and Technology, University of California, Davis, California 95616 monoclonal antibodies in conjunction with immunological and electron microscopic techniques. We find that independent of the ratio of adult to neonatal myosin, depending on the age of the animal, the myosin heavy chains form predominantly homodimeric molecules. The small amount o.
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Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
The functional role of MHC isoforms has been in part clarified by correlated biochemical-physiological studies on single skinned fibers: these studies, in agreement with results from in vitro motility assays, indicate that both MHC and MLC isoforms determine the maximum velocity of shortening of skeletal muscle fibers.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chain (MHC) proteins can be broadly classified into two groups; the sarcomeric (cardiac and skeletal) and nonsarcomeric (smooth muscle and nonmuscle) myosins. The myosin light-chain (MLC) proteins are also classed into two groups, the essential and regulatory light chains.
The functional role of MHC isoforms has been in part clarified by correlated biochemical-physiological studies on single skinned fibers: these studies, in agreement with results from in vitro motility assays, indicate that both MHC and MLC isoforms determine the maximum velocity of shortening of skeletal muscle fibers.
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
The heart muscle is composed of two myosin-heavy chain isoforms: α-cardiac MHC (α-MHC, encoded by MYH6) and β-cardiac MHC (β-MHC, encoded by MYH7). While α-cardiac MHC is mainly expressed in the atrium, expression of β-cardiac MHC is found predominantly in the ventricles (Narolska et al., 2005; Reiser et al., 2001).
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
The functional role of MHC isoforms has been in part clarified by correlated biochemical-physiological studies on single skinned fibers: these studies, in agreement with results from in vitro motility assays, indicate that both MHC and MLC isoforms determine the maximum velocity of shortening of skeletal muscle fibers.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chain (MHC) is the motor protein of muscle thick filaments. Most organisms produce many muscle MHC isoforms with temporally and spatially regulated expression patterns. This suggests that isoforms of MHC have different characteristics necessary for defining specific muscle properties.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chain (MHC) proteins can be broadly classified into two groups; the sarcomeric (cardiac and skeletal) and nonsarcomeric (smooth muscle and nonmuscle) myosins. The myosin light-chain (MLC) proteins are also classed into two groups, the essential and regulatory light chains.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chain (MHC) proteins can be broadly classified into two groups; the sarcomeric (cardiac and skeletal) and nonsarcomeric (smooth muscle and nonmuscle) myosins. The myosin light-chain (MLC) proteins are also classed into two groups, the essential and regulatory light chains.
The heart muscle is composed of two myosin-heavy chain isoforms: α-cardiac MHC (α-MHC, encoded by MYH6) and β-cardiac MHC (β-MHC, encoded by MYH7). While α-cardiac MHC is mainly expressed in the atrium, expression of β-cardiac MHC is found predominantly in the ventricles (Narolska et al., 2005; Reiser et al., 2001).
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chain (MHC) is the motor protein of muscle thick filaments. Most organisms produce many muscle MHC isoforms with temporally and spatially regulated expression patterns. This suggests that isoforms of MHC have different characteristics necessary for defining specific muscle properties.
The heart muscle is composed of two myosin-heavy chain isoforms: α-cardiac MHC (α-MHC, encoded by MYH6) and β-cardiac MHC (β-MHC, encoded by MYH7). While α-cardiac MHC is mainly expressed in the atrium, expression of β-cardiac MHC is found predominantly in the ventricles (Narolska et al., 2005; Reiser et al., 2001).
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
Myosin heavy chain (MHC) is the motor protein of muscle thick filaments. Most organisms produce many muscle MHC isoforms with temporally and spatially regulated expression patterns. This suggests that isoforms of MHC have different characteristics necessary for defining specific muscle properties.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
The functional role of MHC isoforms has been in part clarified by correlated biochemical-physiological studies on single skinned fibers: these studies, in agreement with results from in vitro motility assays, indicate that both MHC and MLC isoforms determine the maximum velocity of shortening of skeletal muscle fibers.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chain (MHC) proteins can be broadly classified into two groups; the sarcomeric (cardiac and skeletal) and nonsarcomeric (smooth muscle and nonmuscle) myosins. The myosin light-chain (MLC) proteins are also classed into two groups, the essential and regulatory light chains.
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
The heart muscle is composed of two myosin-heavy chain isoforms: α-cardiac MHC (α-MHC, encoded by MYH6) and β-cardiac MHC (β-MHC, encoded by MYH7). While α-cardiac MHC is mainly expressed in the atrium, expression of β-cardiac MHC is found predominantly in the ventricles (Narolska et al., 2005; Reiser et al., 2001).
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chain (MHC) is the motor protein of muscle thick filaments. Most organisms produce many muscle MHC isoforms with temporally and spatially regulated expression patterns. This suggests that isoforms of MHC have different characteristics necessary for defining specific muscle properties.
Myosin heavy chains (MyHCs) are ubiquitous actin-based motor proteins that convert the chemical energy derived from hydrolysis of ATP into mechanical force that drives diverse motile processes including cytokinesis, vesicular transport, and cellular locomotion in eukaryotic cells.
Myosin heavy chains account for ~1% of total myocyte protein. They are large molecules of >200,000kDa, organized into two functional domains: an amino terminal globular head that interacts with actin and a carboxyl terminal rod (53,54). Force is transduced via a hinge region between these two domains.
Myosin heavy chain isoforms are an important component defining fiber type specific properties in skeletal muscle, such as oxidative versus glycolytic metabolism, rate of contraction, and fatigability.
5B4 Related content
Neonatal and adult myosin heavy chains form...
by S Lowey · Cited by 33 — The question of whether neonatal and adult myosin isoforms...
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to Neonatal And Adult Myosin Heavy Chains Form Homodimers During ... - Jcb Rupress
Homodimers
epitopes
ELISA
5C3
1983
myosins
1986
5B4
biol
posthatch
Heterodimers
2E9
monoclonal
heterodimer
immunoadsorbent
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