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PMID: 14381426 Published · ppublish English Journal Article

Cell structure and the metabolism of insect flight muscle.

The Journal of biophysical and biochemical cytology ·Vol. 1 ·No. 1 ·1955-01-00 ·Pages 29-46

SACKTOR B

Abstract

The biochemical properties of insect flight muscle were investigated to ascertain the mechanisms whereby energy is made available for the contractile processes. It was found: 1. The endogenous respiration of muscle homogenates was diminished by starving the flies. The substrate for this respiration was probably glycogen. 2. To obtain the maximal rate of oxidation of glucose, the homogenate had to be fortified with inorganic phosphate, Mg ions, ATP, and cytochrome c. The nucleotides, AMP and ADP, were not as effective as ATP. The addition of DPN or TPN was not necessary for this system. 3. Flight muscle homogenates oxidized glycogen, some sugars, and amino acids, as well as the intermediates of the glycolytic and tricarboxylic acid cycles. Other evidence demonstrated the substrate specificity of the muscle. 4. By centrifugation, the muscle homogenate was divided into two fractions: one, a soluble fraction representing the sarcoplasm; the other, the particulate fraction which contained the fibrils and the sarcosomes. 5. The particulate fraction, alone, oxidized all the citric acid cycle intermediates, alpha-glycerophosphate, phosphopyruvate, and the amino acids, glutamic, proline, and cysteine. Regardless of the substrate, no oxygen uptake was found with the sarcoplasm by itself. 6. A recombination of the sarcoplasm and the particulate component was required for the oxidation of glycogen, the hexoses, and all the phosphorylated intermediates of glycolysis, except phosphopyruvate. 7. Isolated mitochondria accounted for all the enzymatic activity of the particulate fraction. These results demonstrate that the enzymes of intermediate metabolism are localized in the sarcoplasm or sarcosomes. The third cytological entity, the myofibrils, plays no role in the energy-providing scheme. From a functional viewpoint, the sarcoplasm and the mitochondria, in combination, furnish the energy for the actomyosin contraction. The results are discussed in relation to analogous findings in other insects and vertebrates.

Keywords
FLIES MUSCLES
MeSH Terms
Amino Acids Animals Citric Acid Cycle Diptera Glycerophosphates Glycogen Glycolysis Insecta Mitochondria Mitochondria, Muscle Muscle Contraction Muscles Myofibrils Oxidation-Reduction
Chemicals
Amino Acids Glycerophosphates Glycogen alpha-glycerophosphoric acid
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
SACKTOR B
References (15)
15 references, click to expand
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Article Info
Journal
The Journal of biophysical and biochemical cytology
Abbr.
J Biophys Biochem Cytol
ISSN
0095-9901
Published
1955-01-00
Pages
29-46
Language
English
Region
United States
NLM ID
17840020R
PMCID
PMC2223591
Subset
OM
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