Optical Ellipsometry Studies on the Diffracted Orders of Single Fibers from Skeletal Muscles

2021 ◽  
pp. 123-148
Author(s):  
Y. Yeh ◽  
R. J. Baskin
Keyword(s):  
Skeletal Muscles ◽  
Single Fibers ◽  
Optical Ellipsometry

scholarly journals Optical Ellipsometry Measurements on the Diffraction Patterns from Single Fibers

1986 ◽  
Vol 49 (1) ◽  
pp. 43-44 ◽  
Author(s):  
R.J. Baskin ◽  
K. Burton ◽  
J.S. Chen ◽  
Y. Yeh
Keyword(s):  
Single Fibers ◽  
Optical Ellipsometry ◽  
Diffraction Patterns

Distribution of tropomyosin isoforms in different types of single fibers isolated from bovine skeletal muscles

Meat Science ◽  
2016 ◽  
Vol 118 ◽  
pp. 129-132 ◽  
Author(s):  
M. Oe ◽  
K. Ojima ◽  
I. Nakajima ◽  
K. Chikuni ◽  
M. Shibata ◽  
...  
Keyword(s):  
Skeletal Muscles ◽  
Single Fibers ◽  
Tropomyosin Isoforms ◽  
Different Types

scholarly journals The use of SUnSET as a non‐radioactive method for measuring rates of protein synthesis in whole skeletal muscles and in single fibers

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Craig Andrew Goodman ◽  
Danielle M. Mabrey ◽  
John W. Frey ◽  
Hannah C. Lincoln ◽  
Man Hing Miu ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Skeletal Muscles ◽  
Single Fibers

Distribution of c-protein isoforms in sarcomeres of developing chick skeletal muscle

1988 ◽  
Vol 46 ◽  
pp. 226-227
Author(s):  
D. A. Fischman ◽  
J. E. Dennis ◽  
T. Obinata ◽  
H. Takano-Ohmuro
Keyword(s):  
Skeletal Muscles ◽  
Thick Filament ◽  
Protein Isoforms ◽  
Actin Binding ◽  
Striated Muscles ◽  
C Protein ◽  
Sarcomeric Protein ◽  
Thick Filaments ◽  
Cross Bridges ◽  
Bridge Bearing

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.

The effect of ionophore A23178 on the α-actinin crosslinks in the z-band of frog skeletal muscle: An EM study

1986 ◽  
Vol 44 ◽  
pp. 154-155
Author(s):  
F.T. Llados ◽  
V. Krlho ◽  
G.D. Pappas
Keyword(s):  
Muscle Damage ◽  
Transmitter Release ◽  
Skeletal Muscles ◽  
Calcium Uptake ◽  
Muscle Membrane ◽  
Frog Skeletal Muscle ◽  
Ach Release ◽  
Sustained Action ◽  
Calcium Deposits ◽  
Intense Stimulation

It Is known that Ca++ enters the muscle fiber at the junctional area during the action of the neurotransmitter, acetylcholine (ACh). Pappas and Rose demonstrated that following Intense stimulation, calcium deposits are found In the postsynaptic muscle membrane, Indicating the existence of calcium uptake In the postsynaptic area following ACh release. In addition to this calcium uptake, when mammal Ian skeletal muscles are exposed to a sustained action of the neurotransmitter, muscle damage develops. These same effects, l.e., Increased transmitter release, calcium uptake and finally muscle damage, can be obtained by Incubating the muscle with lonophore A23178.

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