The Differential Fragmentation of Rabbit Skeletal-Muscle Membrane Systems during Homogenization

1975 ◽  
Vol 3 (6) ◽  
pp. 1248-1251 ◽  
Author(s):  
EDWARD J. BARRETT ◽  
DENIS R. HEADON
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Muscle Membrane ◽  
Membrane Systems

scholarly journals Progressive Structural Defects in Canine Centronuclear Myopathy Indicate a Role for HACD1 in Maintaining Skeletal Muscle Membrane Systems

2017 ◽  
Vol 187 (2) ◽  
pp. 441-456 ◽  
Author(s):  
Gemma L. Walmsley ◽  
Stéphane Blot ◽  
Kerrie Venner ◽  
Caroline Sewry ◽  
Jocelyn Laporte ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Structural Defects ◽  
Muscle Membrane ◽  
Centronuclear Myopathy ◽  
Membrane Systems

High-affinity [3H]PN200-110 and [3H]ryanodine binding to rabbit and frog skeletal muscle

1994 ◽  
Vol 266 (2) ◽  
pp. C462-C466 ◽  
Author(s):  
K. Anderson ◽  
A. H. Cohn ◽  
G. Meissner
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Muscle Membrane ◽  
Scatchard Analysis ◽  
Physical Interaction ◽  
Frog Skeletal Muscle ◽  
Release Channel ◽  
High Affinity ◽  
Voltage Dependent ◽  
Student’S T

In vertebrate skeletal muscle, the voltage-dependent mechanism of sarcoplasmic reticulum (SR) Ca2+ release, commonly referred to as excitation-contraction (E-C) coupling, is mediated by the voltage-sensing dihydropyridine receptor (DHPR), which is believed to affect SR Ca2+ release through a physical interaction with the SR ryanodine receptor (RYR)/Ca2+ release channel. Scatchard analysis of ligand binding of [3H]PN200-110 to the DHPR and [3H]ryanodine to the RYR indicated the presence of high-affinity sites in muscle homogenates, with maximum binding (Bmax) values of 72 +/- 26 and 76 +/- 30 pmol/g wet wt for rabbit skeletal muscle, and 27 +/- 14 and 44 +/- 13 pmol/g wet wt for frog skeletal muscle, respectively. The Bmax values corresponded to a PN200-110-to-ryanodine binding ratio of 0.98 +/- 0.26 and 0.61 +/- 0.24 for rabbit and frog skeletal muscle, respectively, and were found by Student's t test to be significantly different (P < 0.02, n = 7). These results are compared with measurements with isolated rabbit skeletal muscle membrane fractions and discussed in relation to our current understanding of the mechanism of E-C coupling in skeletal muscle.

scholarly journals The Reduction in Vitro of 17α-Hydroxypregnenolone (3β,17α-Dihydroxy-Δ5-pregnen-20-one) by Rabbit Skeletal Muscle

1960 ◽  
Vol 235 (10) ◽  
pp. 2797-2800
Author(s):  
Patricia Z. Thomas ◽  
Enrico Forchielli ◽  
Ralph I. Dorfman
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle

scholarly journals Characterization of rabbit skeletal muscle glycogenin. Tyrosine 194 is essential for function

1993 ◽  
Vol 268 (20) ◽  
pp. 14687-14693 ◽  
Author(s):  
Y. Cao ◽  
A.M. Mahrenholz ◽  
A.A. DePaoli-Roach ◽  
P.J. Roach
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle
Sign in / Sign up

Export Citation Format

Share Document