Myosin heavy chains in fast skeletal muscle of chick embryo

1981 ◽  
Vol 37 (12) ◽  
pp. 1268-1270 ◽  
Author(s):  
L. Dalla Libera
Keyword(s):  
Skeletal Muscle ◽  
Chick Embryo ◽  
Myosin Heavy Chains ◽  
Fast Skeletal Muscle ◽  
Heavy Chains

Three Slow Myosin Heavy Chains Sequentially Expressed in Developing Mammalian Skeletal Muscle

1993 ◽  
Vol 158 (1) ◽  
pp. 183-199 ◽  
Author(s):  
Simon M. Hughes ◽  
Mildred Cho ◽  
Ilene Karsch-Mizrachi ◽  
Marilyn Travis ◽  
Laura Silberstein ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mammalian Skeletal Muscle ◽  
Myosin Heavy Chains ◽  
Slow Myosin ◽  
Heavy Chains

scholarly journals Neonatal and adult myosin heavy chains form homodimers during avian skeletal muscle development.

1991 ◽  
Vol 113 (2) ◽  
pp. 303-310 ◽  
Author(s):  
S Lowey ◽  
G S Waller ◽  
E Bandman
Keyword(s):  
Skeletal Muscle ◽  
Muscle Development ◽  
Coiled Coil ◽  
Myosin Isoforms ◽  
Myosin Heavy Chains ◽  
Electron Microscopic ◽  
Hybrid Species ◽  
Heavy Chains ◽  
Stage Of Development ◽  
Microscopic Techniques

Myosin isoforms contribute to the heterogeneity and adaptability of skeletal muscle fibers. Besides the well-characterized slow and fast muscle myosins, there are those isoforms that appear transiently during the course of muscle development. At a stage of development when two different myosins are coexpressed, the possibility arises for the existence of heterodimers, molecules containing two different heavy chains, or homodimers, molecules with two identical heavy chains. The question of whether neonatal and adult myosin isoforms can associate to form a stable heterodimer was addressed by using stage-specific 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 of hybrid species present suggests that either the rod portion of the two heavy chain isoforms differs too much in sequence to form a stable alpha-helical coiled coil, or that the biosynthesis of the heavy chains precludes the formation of heterodimeric molecules.

scholarly journals Incorporation of myosin heavy chains into the A‐bands of living skeletal muscle cells

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Joseph W Sanger ◽  
Jushuo Wang ◽  
Yingli Fan ◽  
Balraj Mittal ◽  
Jean M Sanger
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Myosin Heavy Chains ◽  
Heavy Chains

Effect of Hypophysectomy and Growth Hormone Administration on Myosin Heavy Chains in Rat Skeletal Muscle

2004 ◽  
Vol 36 (Supplement) ◽  
pp. S302
Author(s):  
Daniel A. Judelson ◽  
William J. Kraemer ◽  
Nicholas A. Demonaco ◽  
Barry A. Spiering ◽  
Ricardo Silvestre ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Growth Hormone ◽  
Myosin Heavy Chains ◽  
Rat Skeletal Muscle ◽  
Growth Hormone Administration ◽  
Heavy Chains ◽  
Hormone Administration

scholarly journals Role of myosin heavy chains from rabbit skeletal muscle in the heat-induced gelation mechanism.

1984 ◽  
Vol 48 (9) ◽  
pp. 2225-2232 ◽  
Author(s):  
Kunihiko SAMEJIMA ◽  
Hiroshi YAMAUCHI ◽  
Ali ASGHAR ◽  
Tsutomu YASUI
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Myosin Heavy Chains ◽  
Gelation Mechanism ◽  
Heavy Chains
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