Myosin Heavy Chains
Mostrando 13-24 de 87 artigos, teses e dissertações.
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13. Contractile protein isozymes in muscle development: identification of an embryonic form of myosin heavy chain.
The nature of the myosin heavy chain in embryonic muscle tissue, cultured muscle cells, and several adult muscles was investigated. After denaturation with sodium dodecyl sulfate, purified rat myosins were subjected to partial proteolytic cleavage or immunological analysis using microcomplement fixation. Three types of myosin heavy chains could be demonstrat
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14. Cardiac alpha-myosin heavy chains differ in their induction of myocarditis. Identification of pathogenic epitopes.
BALB/c mice develop autoimmune myocarditis after immunization with mouse cardiac myosin, whereas C57B/6 mice do not. To define the immunogenicity and pathogenicity of cardiac myosin in BALB/c mice, we immunized mice with different forms of cardiac myosin. These studies demonstrate the discordance of immunogenicity and pathogenicity of myosin heavy chains. Th
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15. Erratum: Identification of the gene for fly non-muscle myosin heavy chain: Drosophila myosin heavy chains are encoded by a gene family
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16. Myosin Heavy Chain Messenger RNA from Myogenic Cell Cultures
The appearance of messenger RNA for myosin heavy chains in chick-embryo myogenic cell cultures was investigated. Total polyribosomes were isolated from cultures at various times of development and were purified in sucrose step gradients. These polysomes were either extracted with phenol or were treated with puromycin. The ribonucleoprotein particles and ribo
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17. Mutants altering coordinate synthesis of specific myosins during nematode muscle development.
Mutations in the unc-52 gene on linkage group II retard the construction of body-wall muscle sarcomeres during larval development in the nematode Caenorhabditis elegans. Unc-52 mutants show decreased accumulation of myosin heavy chains relative to other polypeptides during larval development, correlating with the structural retardation. Pulse radiolabeling e
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18. Human cardiac myosin heavy chain genes and their linkage in the genome.
Human myosin heavy chains are encoded by a multigene family consisting of at least 10 members. A gene-specific oligonucleotide has been used to isolate the human beta myosin heavy chain gene from a group of twelve nonoverlapping genomic clones. We have shown that this gene (which is expressed in both cardiac and skeletal muscle) is located 3.6kb upstream of
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19. Functional chicken gizzard heavy meromyosin expression in and purification from baculovirus-infected insect cells.
The heavy chain and the essential and the regulatory light chains of chicken gizzard heavy meromyosin (HMM) were coexpressed in Spodoptera frugiperda (fall armyworm) cells infected with a mixture of two recombinant Autographa californica baculoviruses. Soluble HMM consisting of the heavy chain and the two types of light chains was obtained. The recombinant H
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20. Adult fast myosin pattern and Ca2+-induced slow myosin pattern in primary skeletal muscle culture
A primary muscle cell culture derived from newborn rabbit muscle and growing on microcarriers in suspension was established. When cultured for several weeks, the myotubes in this model develop the completely adult pattern of fast myosin light and heavy chains. When Ca2+ ionophore is added to the culture medium on day 11, raising intracellular [Ca2+] about 10
The National Academy of Sciences of the USA.
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21. Immunofluorescence analysis of the primordial myosin detectable in embryonic striated muscle.
Immunofluorescence analysis showed that the earliest myosin detectable in both the embryonic chicken heart and somitic myotome, the precursor to skeletal muscle, was strongly reactive with two different monoclonal antibodies specific for the heavy chain of cardiac ventricular myosin, but it showed no reactivity with affinity-purified polyclonal antibodies sp
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22. Functional analysis of the mutations in the human cardiac beta-myosin that are responsible for familial hypertrophic cardiomyopathy. Implication for the clinical outcome.
More than 30 missense mutations in the beta-cardiac myosin heavy chain gene have been shown to be responsible for familial hypertrophic cardiomyopathy. To clarify the effects of these point mutations on myosin motor function, we expressed wild-type and mutant human beta-cardiac myosin heavy chains in insect cells with human cardiac light chains. The wild-typ
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23. Snythesis of polypeptides with the properties of myosin light chains direct by RNA extracted from muscle cultures.
Polyadenylylated RNA, extracted from differentiating primary cultures of rat muscle and the myogenic cell line L8, directs the synthesis of polypeptides in the wheat germ cell-free system which comigrate with myosin light chains under several electrophoretic conditions. The peptides also associate specifically with heavy myosin subunits during dissociation-r
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24. Unshadowed myosin molecules: STEM mass-maps of myosin heads.
Myosin molecules were directly visualized without heavy metal shadowing by scanning transmission electron microscopy (STEM) under low dose conditions. The general appearance and dimensions of heavy metal-free molecules were similar to those of shadowed myosin, either after freeze-drying without or air-drying with glycerol. Two characteristic configurations o