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Electrophoretic Separation And Immunological Identification Of Type 2X Myosin Heavy Chain In Rat Skeletal Muscle.

W. LaFramboise, M. Daood, R. Guthrie, P. Moretti, S. Schiaffino, M. Ontell
Published 1990 · Biology, Medicine

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One slow and three fast myosin heavy chains have been described in typical skeletal muscles of the adult rat using immunocytochemical analysis. Electrophoretic isolation and immunochemical identification of these four isoforms has not been achieved. An electrophoretic procedure is described which, by altering the cross-linkage and polymerization kinetics of 5% polyacrylamide gels, allows resolution of these four distinct myosin heavy chains. Using specific monoclonal antibodies and double immunoblotting analysis, the identity and electrophoretic migration order of the myosin heavy chains was established to be: 2A less than 2X less than 2B less than beta/slow.
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This paper is referenced by
Force-velocity and power cnaraccenstics muscle fibers after hindlimb suspension
K. McDonald (1994)
Murgia Muscle Diversity and Plasticity Activity-Dependent Signaling Pathways Controlling
S. Schiaffino (2007)
10.1172/JCI117795
Abnormal contractile properties of muscle fibers expressing beta-myosin heavy chain gene mutations in patients with hypertrophic cardiomyopathy.
E. B. Lankford (1995)
10.1002/PPUL.1950160504
Regional Distribution of Myosin Heavy Chain Isoforms in Rib Cage Muscles as a Function of Postnatal Development
R. L. Vazquez (1993)
10.1002/1097-010X(20010101/31)289:1<10::AID-JEZ2>3.0.CO;2-R
Muscle phenotype remains unaltered after limb autotomy and unloading.
B. Griffis (2001)
10.1016/0012-1606(91)90473-G
Emergence of the mature myosin phenotype in the rat diaphragm muscle.
W. LaFramboise (1991)
10.1152/japplphysiol.00347.2007
Developmental effects on myonuclear domain size of rat diaphragm fibers.
C. Mantilla (2008)
10.1152/JAPPLPHYSIOL.01091.2002
Effect of hindlimb suspension on the functional properties of slow and fast soleus fibers from three strains of mice.
J. E. Stelzer (2003)
10.1111/J.1432-1033.1997.00030.X
Quantitative analyses of myosin heavy-chain mRNA and protein isoforms in single fibers reveal a pronounced fiber heterogeneity in normal rabbit muscles.
H. Peuker (1997)
10.1111/J.1748-1716.1993.TB09493.X
An age-related type IIB to IIX myosin heavy chain switching in rat skeletal muscle.
L. Larsson (1993)
10.1046/J.1365-201X.1998.0284F.X
Hindlimb suspension induces the expression of multiple myosin heavy chain isoforms in single fibres of the rat soleus muscle.
Y. Oishi (1998)
10.1139/Z98-158
Histochemical and electrophoretic analysis of the primary flight muscle of several phyllostomid bats
J. Hermanson (1998)
10.1002/(SICI)1097-010X(20000101)286:1<36::AID-JEZ4>3.0.CO;2-G
Muscle type-specific myosin isoforms in crustacean muscles.
W. LaFramboise (2000)
diaphragm: coexpression patterns and effect of COPD Developmental myosin heavy chains in the adult human
Sanford Levine (2013)
10.1111/J.1748-1716.1992.TB09315.X
Myosin heavy chain isoform transition in ageing fast and slow muscles of the rat.
T. Sugiura (1992)
10.1083/JCB.121.4.795
Evidence for myoblast-extrinsic regulation of slow myosin heavy chain expression during muscle fiber formation in embryonic development
M. Cho (1993)
A study of biochemical and physiological properties of normal and functionally impaired skeletal muscles
S. K. Bortolotto (2000)
10.1016/0197-0186(95)00014-Y
In vitro myoblast to myotube transformations in the presence of leukemia inhibitory factor
N. Vakakis (1995)
10.1016/S1095-6433(00)00270-1
Sensitivity of transformed (phasic to tonic) motor neurons to the neuromodulator 5-HT.
B. Griffis (2000)
10.1007/978-1-4615-2872-2_66
Two classes of mammalian skeletal muscle fibers distinguished by metabolite content.
M. Kushmerick (1993)
10.1016/0012-1606(92)90010-E
Structural and developmental analysis of two linked myosin heavy chain genes.
J. Parker-Thornburg (1992)
10.1152/JAPPL.1998.84.6.1967
Cellular adaptations of skeletal muscles to cyclosporine.
M. S. Biring (1998)
10.1152/AJPCELL.1995.268.2.C419
Sensitive detection of myosin heavy chain composition in skeletal muscle under different loading conditions.
S. Fauteck (1995)
10.1152/AJPCELL.1997.273.2.C588
Functional properties of conditioned skeletal muscle: implications for muscle-powered cardiac assist.
D. Trumble (1997)
10.1056/NEJM199712183372503
Cellular adaptations in the diaphragm in chronic obstructive pulmonary disease.
S. Levine (1997)
10.1152/AJPCELL.1991.261.1.C93
MHC composition and enzyme-histochemical and physiological properties of a novel fast-twitch motor unit type.
L. Larsson (1991)
10.1071/RD9951361
The developmental switch in ventricular myosin expression in vivo is not triggered by an increase in cyclic AMP.
F. Schachat (1995)
10.1152/PHYSIOL.00009.2007
Activity-dependent signaling pathways controlling muscle diversity and plasticity.
S. Schiaffino (2007)
10.17221/2270-CJAS
Pattern of fibre type distribution within muscle fascicles of pigs (Sus scrofa domestica)
Dejan Škorjanc (2018)
10.1016/0304-3940(92)90899-I
Reinnervation of denervated extensor digitorum longus of the rat by the nerve of the soleus does not induce the type I myosin synthesis directly but through a sequential transition of type II myosin isoforms
Jean-Claude Mira (1992)
10.1152/AJPCELL.1996.270.4.C1236
Contractile and metabolic effects of increased creatine kinase activity in mouse skeletal muscle.
B. Roman (1996)
10.1002/ELPS.1150181115
A sensitive electrophoretic method for the quantification of myosin heavy chain isoforms in horse skeletal muscle: Histochemical and immunocytochemical verifications
J. L. Rivero (1997)
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