The Synthesis of Myosin, Actin and the Major Protein Fractions in Rabbit Skeletal Muscle

Overview

Journal Biochem J

Specialty Biochemistry

Date 1979 Sep 15

PMID 518569

Citations 6

Authors

G E Lobley

J M Lovie

Affiliations

Soon will be listed here.

Abstract

New Zealand White rabbits were infused with [3H]tyrosine for periods of 5--6 h and then different methods of extraction were applied for the purification of the main muscle proteins and protein fractions. Myosin (I), prepared from salt extraction of muscle mince, consistently had a higher specific radioactivity than did myosin (II), isolated by dissociation of actomyosin. Actins (IA) and (IB), extracted from acetone-dried powders prepared by different treatments of myosin-extracted muscle mince, gave specific radioactivities approx. 0.6 that of myosin (I) and 0.7 that of myosin(II). Actin (II), isolated by dissociation of actomyosin, had a specific radioactivity similar to that of myosin (II) from the same source, but higher than those of actins (IA) and (IB). The differences between the specific radioactivities of the proteins, in particular actin, purified by the various methods, are attributed to the loss of newly synthesized material of high specific radioactivity during the initial extraction procedures. It is suggested that actin (II) and myosin (II) are representative preparations for the total population of each protein and that, on this basis, myosin and actin have similar rates of synthesis. Total muscle protein, myofibrils, actomyosin and sarcoplasm were all found to have very similar specific radioactivities at the end of a 6 h infusion.

Citing Articles

Reappraisal of the quantitative importance of non-skeletal-muscle source of N tau-methylhistidine in urine.

Harris C Biochem J. 1981; 194(3):1011-4.

PMID: 7306010 PMC: 1162840. DOI: 10.1042/bj1941011.

Measurement of the synthesis rates of collagens and total protein in rabbit muscle.

Palmer R, Robins S, Lobley G Biochem J. 1980; 192(2):631-6.

PMID: 6786281 PMC: 1162379. DOI: 10.1042/bj1920631.

Myofibrillar protein turnover. Synthesis of protein-bound 3-methylhistidine, actin, myosin heavy chain and aldolase in rat skeletal muscle in the fed and starved states.

Bates P, Grimble G, Sparrow M, Millward D Biochem J. 1983; 214(2):593-605.

PMID: 6615482 PMC: 1152286. DOI: 10.1042/bj2140593.

Myofibrillar protein turnover. Synthesis rates of myofibrillar and sarcoplasmic protein fractions in different muscles and the changes observed during postnatal development and in response to feeding and starvation.

Bates P, Millward D Biochem J. 1983; 214(2):587-92.

PMID: 6615481 PMC: 1152285. DOI: 10.1042/bj2140587.

The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle.

Preedy V, Sugden P Biochem J. 1989; 257(2):519-27.

PMID: 2930464 PMC: 1135609. DOI: 10.1042/bj2570519.

References

WINNICK R, WINNICK T . Protein synthesis in skeletal muscle, with emphasis on myofibrils. J Biol Chem. 1960; 235:2657-61. View

VELICK S . The metabolism of myosin, the meromyosins, actin and tropomyosin in the rabbit. Biochim Biophys Acta. 1956; 20(1):228-36. DOI: 10.1016/0006-3002(56)90281-5. View

CARSTEN M, MOMMAERTS W . A study of actin by means of starch gel electrophoresis. Biochemistry. 1963; 2:28-32. DOI: 10.1021/bi00901a006. View

PERRY S, ZYDOWO M . The nature of the extra protein fraction from myofibrils of striated muscle. Biochem J. 1959; 71(2):220-8. PMC: 1196778. DOI: 10.1042/bj0710220. View

Barany M, Barany K, GUBA F . Preparation of actin without extraction of myosin. Nature. 1957; 179(4564):818-9. DOI: 10.1038/179818b0. View

Laurent G, Sparrow M, Millward D . Turnover of muscle protein in the fowl. Changes in rates of protein synthesis and breakdown during hypertrophy of the anterior and posterior latissimus dorsi muscles. Biochem J. 1978; 176(2):407-17. PMC: 1186248. DOI: 10.1042/bj1760407. View

Bilmazes C, Kien C, Rohrbaugh D, Uauy R, Burke J, MUNRO H . Quantitative contribution by skeletal muscle to elevated rates of whole-body protein breakdown in burned children as measured by N tau-methylhistidine output. Metabolism. 1978; 27(6):671-6. DOI: 10.1016/0026-0495(78)90004-5. View

Nicholas G, Lobley G, Harris C . Use of the constant infusion technique for measuring rates of protein synthesis in the New Zealand White rabbit. Br J Nutr. 1977; 38(1):1-17. DOI: 10.1079/bjn19770056. View

Zak R, Martin A, Prior G, Rabinowitz M . Comparison of turnover of several myofibrillar proteins and critical evaluation of double isotope method. J Biol Chem. 1977; 252(10):3430-5. View

10.

Martin A, Rabinowitz M, Blough R, Prior G, Zak R . Measurements of half-life of rat cardiac myosin heavy chain with leucyl-tRNA used as precursor pool. J Biol Chem. 1977; 252(10):3422-9. View

11.

SWICK R, Song H . Turnover rates of various muscle proteins. J Anim Sci. 1974; 38(5):1150-7. DOI: 10.2527/jas1974.3851150x. View

12.

Schaub M, PERRY S . The regulatory proteins of the myofibril. Characterization and properties of the inhibitory factor (troponin B). Biochem J. 1971; 123(3):367-77. PMC: 1176967. DOI: 10.1042/bj1230367. View

13.

Seraydarian K, BRISKEY E, MOMMAERTS W . The modification of actomyosin by alpha- actinin. I. A survey of experimental conditions. Biochim Biophys Acta. 1967; 133(3):399-411. DOI: 10.1016/0005-2795(67)90544-2. View

14.

Koizumi T . Turnover rates of structural proteins of rabbit skeletal muscle. J Biochem. 1974; 76(2):431-9. DOI: 10.1093/oxfordjournals.jbchem.a130585. View

15.

Perry B . Protein turnover in skeletal muscle of piglets. Br J Nutr. 1974; 31(1):35-45. DOI: 10.1079/bjn19740006. View

16.

Morkin E, Yazaki Y, Katagiri T, Laraia P . Comparison of the synthesis of the light and heavy chains of adult skeletal myosin. Biochim Biophys Acta. 1973; 324(3):420-9. DOI: 10.1016/0005-2787(73)90286-4. View

17.

Sender P, Garlick P . Synthesis rates of protein in the Langendorff-perfused rat heart in the presence and absence of insulin, and in the working heart. Biochem J. 1973; 132(3):603-8. PMC: 1177625. DOI: 10.1042/bj1320603. View

18.

Low R, GOLDBERG A . Nonuniform rates of turnover of myofibrillar proteins in rat diaphragm. J Cell Biol. 1973; 56(2):590-5. PMC: 2108896. DOI: 10.1083/jcb.56.2.590. View

19.

Morkin E . Postnatal muscle fiber assembly: localization of newly synthesized myofibrillar proteins. Science. 1970; 167(3924):1499-501. DOI: 10.1126/science.167.3924.1499. View

20.

Etlinger J, Zak R, Fischman D, Rabinowitz M . Isolation of newly synthesised myosin filaments from skeletal muscle homogenates and myofibrils. Nature. 1975; 255(5505):259-61. DOI: 10.1038/255259a0. View