scholarly journals The role of creatine kinase and arginine kinase in muscle

1978 ◽  
Vol 172 (3) ◽  
pp. 533-537 ◽  
Author(s):  
E A Newsholme ◽  
I Beis ◽  
A R Leech ◽  
V A Zammit
Keyword(s):  
Creatine Kinase ◽  
Maximum Rate ◽  
Skeletal Muscles ◽  
Flight Muscle ◽  
Insect Flight ◽  
Arginine Kinase ◽  
Maximum Activity ◽  
Insect Flight Muscle ◽  
Atp Turnover

Arginine and creatine kinase activities in different muscles are compared with calculated maximum rates of ATP turnover. The magnitude of the kinase activities decreases in the following order: anaerobic muscles and vertebrate skeletal muscles greater than heart muscle greater than insect flight muscle. The maximum activity of phosphagen kinases (i.e. creatine kinase and arginine kinase), in the direction of phosphagen formation, is lower than the calculated maximum rate of ATP turnover in insect flight muscle or rat heart.

On the role of arginine kinase in insect flight muscle

1989 ◽  
Vol 19 (5) ◽  
pp. 471-480 ◽  
Author(s):  
A. Schneider ◽  
R.J. Wiesner ◽  
M.K. Grieshaber
Keyword(s):  
Flight Muscle ◽  
Insect Flight ◽  
Arginine Kinase ◽  
Insect Flight Muscle

Role of fatty acid-binding protein in lipid metabolism of insect flight muscle

1993 ◽  
Vol 123 (1-2) ◽  
pp. 145-152 ◽  
Author(s):  
Dick J. van der Horst ◽  
Jan M. van Doorn ◽  
Paul C. C. M. Passier ◽  
Michael M. Vork ◽  
Jan F. C. Glatz
Keyword(s):  
Fatty Acid ◽  
Lipid Metabolism ◽  
Fatty Acid Binding Protein ◽  
Flight Muscle ◽  
Insect Flight ◽  
Binding Protein ◽  
Insect Flight Muscle ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Role of fatty acid-binding protein in lipid metabolism of insect flight muscle

1993 ◽  
pp. 145-152
Author(s):  
Dick J. van der Horst ◽  
Jan M. van Doorn ◽  
Paul C. C. M. Passier ◽  
Michael M. Vork ◽  
Jan F. C. Glatz
Keyword(s):  
Fatty Acid ◽  
Lipid Metabolism ◽  
Fatty Acid Binding Protein ◽  
Flight Muscle ◽  
Insect Flight ◽  
Binding Protein ◽  
Insect Flight Muscle ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals The activities of phosphorylase, hexokinase, phosphofructokinase, lactate dehydrogenase and the glycerol 3-phosphate dehydrogenase in muscles from vertebrates and invertebrates

1972 ◽  
Vol 126 (1) ◽  
pp. 49-58 ◽  
Author(s):  
B. Crabtree ◽  
E. A. Newsholme
Keyword(s):  
White Muscle ◽  
Flight Muscle ◽  
Insect Flight ◽  
Maximum Activity ◽  
Glycolytic Flux ◽  
Insect Flight Muscle ◽  
Glycerophosphate Dehydrogenase ◽  
Vertebrate Muscle ◽  
Activity Measurements ◽  
Glycerol 3 Phosphate Dehydrogenase

1. The maximum activities of hexokinase, phosphorylase and phosphofructokinase have been measured in extracts from a variety of muscles and they have been used to estimate the maximum rates of operation of glycolysis in muscle. These estimated rates of glycolysis are compared with those calculated for the intact muscle from such information as oxygen uptake, glycogen degradation and lactate formation. Reasonable agreement between these determinations is observed, and this suggests that such enzyme activity measurements may provide a useful method for comparative investigations into quantitative aspects of maximum glycolytic flux in muscle. 2. The enzyme activities from insect flight muscle confirm and extend much of the earlier work and indicate the type of fuel that can support insect flight. The maximum activity of hexokinase in some insect flight muscles is about tenfold higher than that in vertebrate muscles. The activity of phosphorylase is greater, in general, in vertebrate muscle (particularly white muscle) than in insect flight muscle. This is probably related to the role of glycogen breakdown in vertebrate muscle (particularly white muscle) for the provision of ATP from anaerobic glycolysis and not from complete oxidation of the glucose residues. The activity of hexokinase was found to be higher in red than in white vertebrate muscle, thus confirming and extending earlier reports. 3. The maximum activity of the mitochondrial glycerophosphate dehydrogenase was always much lower than that of the cytoplasmic enzyme, indicating that the former enzyme is rate-limiting for the glycerol 3-phosphate cycle. From the maximum activity of the mitochondrial enzyme it can be calculated that the operation of this cycle would account for the reoxidation of all the glycolytically produced NADH in insect flight muscle but it could account for only a small amount in vertebrate muscle. Other mechanisms for this NADH reoxidation in vertebrate muscle are discussed briefly.

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