scholarly journals Determination of Primary Structure of Heavy Meromyosin Region of Walleye Pollack Myosin Heavy Chain by cDNA Cloning

1998 ◽  
Vol 64 (5) ◽  
pp. 812-819 ◽  
Author(s):  
Takao Ojima ◽  
Nagako Kawashima ◽  
Akira Inoue ◽  
Akiko Amauchi ◽  
Marie Togashi ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Cdna Cloning ◽  
Heavy Chain ◽  
Primary Structure ◽  
Heavy Meromyosin ◽  
Walleye Pollack

cDNA cloning of myosin rod and the complete primary structure of myosin heavy chain of walleye pollack fast skeletal muscle

2000 ◽  
Vol 66 (2) ◽  
pp. 349-357 ◽  
Author(s):  
M ARIE TOGASHI ◽  
M AKOTO KAKINUMA ◽  
Y ASUSHI HIRAYAMA ◽  
H IDETO FUKUSHIMA ◽  
S HUGO WATABE ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Cdna Cloning ◽  
Heavy Chain ◽  
Primary Structure ◽  
Fast Skeletal Muscle ◽  
Walleye Pollack ◽  
Myosin Rod ◽  
Complete Primary Structure

scholarly journals Isolation of human skeletal muscle myosin heavy chain and actin for measurement of fractional synthesis rates

1998 ◽  
Vol 275 (6) ◽  
pp. E1092-E1099 ◽  
Author(s):  
D. L. Hasten ◽  
G. S. Morris ◽  
S. Ramanadham ◽  
K. E. Yarasheski
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Sodium Dodecyl ◽  
Synthesis Rate ◽  
Simple Method ◽  
Skeletal Muscle Myosin ◽  
Fractional Synthesis

Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60–80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates. The amounts of MHC and actin isolated are adequate for the quantification of [13C]leucine abundance by gas chromatography-combustion-isotope ratio mass spectrometry (GC-C-IRMS). Fractional synthesis rates of mixed muscle protein (MMP), MHC, and actin were determined in six healthy young subjects (27 ± 1 yr) after they received a 14-h intravenous infusion (prime = 7.58 μmol/kg body wt, constant infusion = 7.58 μmol ⋅ kg body wt−1 ⋅ h−1) of [1-13C]leucine. The fractional synthesis rates of MMP, MHC, and actin were found to be 0.0468 ± 0.0048, 0.0376 ± 0.0033, and 0.0754 ± 0.0078%/h, respectively. Overall, the synthesis rate of MHC was 20% lower ( P = 0.012), and the synthesis rate of actin was 61% higher ( P = 0.060, not significant) than the MMP synthesis rate. The isolation of these proteins for isotope abundance analysis by GC-C-IRMS provides important information about the synthesis rates of these specific contractile proteins, as opposed to the more general information provided by the determination of MMP synthesis rates.

Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence

1987 ◽  
Vol 198 (2) ◽  
pp. 143-157 ◽  
Author(s):  
Masashi Yanagisawa ◽  
Yoshio Hamada ◽  
Yoshinari Katsuragawa ◽  
Michihiro Imamura ◽  
Takashi Mikawa ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Myosin Heavy Chain ◽  
Dna Sequence ◽  
Heavy Chain ◽  
Primary Structure ◽  
Smooth Muscle Myosin ◽  
Complementary Dna ◽  
Muscle Myosin ◽  
Complete Primary Structure
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