Artigo Revisado por pares

THE EFFECT OF AGING ON PHYSICOCHEMICAL PROPERTIES OF ACTOMYOSIN FROM CHICKEN BREAST AND LEG MUSCLE

1972; Wiley; Volume: 37; Issue: 3 Linguagem: Inglês

10.1111/j.1365-2621.1972.tb02634.x

ISSN

1750-3841

Autores

Joshua Hay, R. W. CURRIE, F.H. Wolfe,

Tópico(s)

Pharmacological Effects and Assays

Resumo

Journal of Food ScienceVolume 37, Issue 3 p. 346-350 THE EFFECT OF AGING ON PHYSICOCHEMICAL PROPERTIES OF ACTOMYOSIN FROM CHICKEN BREAST AND LEG MUSCLE J. D. HAY, J. D. HAY Dept. of Food Science, University of Alberta, Edmonton 7, Alberta, CanadaSearch for more papers by this authorR. W. CURRIE, R. W. CURRIE Dept. of Food Science, University of Alberta, Edmonton 7, Alberta, CanadaSearch for more papers by this authorF. H. WOLFE, F. H. WOLFE Dept. of Food Science, University of Alberta, Edmonton 7, Alberta, CanadaSearch for more papers by this author J. D. HAY, J. D. HAY Dept. of Food Science, University of Alberta, Edmonton 7, Alberta, CanadaSearch for more papers by this authorR. W. CURRIE, R. W. CURRIE Dept. of Food Science, University of Alberta, Edmonton 7, Alberta, CanadaSearch for more papers by this authorF. H. WOLFE, F. H. WOLFE Dept. of Food Science, University of Alberta, Edmonton 7, Alberta, CanadaSearch for more papers by this author First published: May 1972 https://doi.org/10.1111/j.1365-2621.1972.tb02634.xCitations: 20 The authors gratefully acknowledge the financial support of the National Research Council of Canada (grant #NRC A-5751) and the many helpful suggestions of Dr. C.M. Kay and Dr. W.D. McCubbin of the Dept. of Biochemistry. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat REFERENCES Arakawa, N., Robson, R.M. and Goll, D.E. 1970. An improved method for the preparation of α-actinin from rabbit striated muscle. Biochim. Biophys. Acta 200: 284. 10.1016/0005-2795(70)90172-8 CASPubMedGoogle Scholar Bárány, M., Bárány, K., Reckard, T. and Volpe, A. 1965. Myosin of fast and slow muscles of the rabbit. Arch. Biochem. Biophys. 109: 185. 10.1016/0003-9861(65)90304-8 CASPubMedGoogle Scholar Briskey, E.J., Seraydarian, K. and Mommaerts, W.F.H.M. 1967. The modification of actomyosin by α-actinin. 3. The interaction between α-actinin and actin. Biochim. Biophys. Acta 133: 424. 10.1016/0005-2795(67)90546-6 CASPubMedWeb of Science®Google Scholar Buttkus, H. 1970. Accelerated denaturation of myosin in frozen solution. J. Food Sci. 35: 558. 10.1111/j.1365-2621.1970.tb04808.x CASGoogle Scholar Caldwell, K.A. and Lineweaver, H. 1969. Sulfhydryl content of excised chicken breast muscle during post mortem aging. J. Food Sci. 34: 290. 10.1111/j.1365-2621.1969.tb10345.x CASWeb of Science®Google Scholar Chajuss, D. and Spencer, J.V. 1962. Changes in the total sulfhydryl group content and histochemical denaturation of sulfonates in excised chicken muscle aged in air. J. Food Sci. 27: 411. 10.1111/j.1365-2621.1962.tb00117.x Web of Science®Google Scholar Chaudry, H.M., Parrish, F.C. Jr. and Goll, D.E. 1969. Molecular properties of post-mortem muscle. 6. Effect of temperature on protein solubility of rabbit and bovine muscle. J. Food Sci. 34: 183. Google Scholar DeFremery, D. and Pool, M.F. 1960. Biochemistry of chicken muscle as related to tenderness. Food Res. 25: 73. 10.1111/j.1365-2621.1960.tb17938.x CASGoogle Scholar Ellman, G.L. 1958. A calorimetric method for determining low concentrations of mercaptans. Arch. Biochem. Biophys. 74: 443. 10.1016/0003-9861(58)90014-6 CASPubMedWeb of Science®Google Scholar Fujimaki, M., Arakawa, N., Okitani, A. and Takagi, O. 1965a. The changes of "Myosin B" (actomyosin) during storage of rabbit muscle. 2. The dissociation of "Myosin B" into myosin A and actin and its interaction with ATP. J. Food Sci. 30: 937. 10.1111/j.1365-2621.1965.tb01868.x CASWeb of Science®Google Scholar Fujimaki, M., Okitani, A. and Arakawa, N. 1965b. The changes of "Myosin B" during storage of rabbit muscle. 1. Physico-chemical studies on "Myosin B". Agric. Biol. Chem. 29: 581. 10.1271/bbb1961.29.581 CASWeb of Science®Google Scholar Fujimaki, M., Arakawa, N., Okitani, A. and Takagi, O. 1965c. The dissociation of "Myosin B" from the stored rabbit muscle into myosin A and actin and its interaction with ATP. Agric. Biol. Chem. 29: 700. 10.1271/bbb1961.29.700 CASWeb of Science®Google Scholar Gawronski, T.H., Spencer, J.V. and Pubols, M.H. 1967. Changes in sulfhydryl and disulfide content of chicken muscle and the effect of N-ethylmaleimide. J. Agr. Food Chem. 15: 781. 10.1021/jf60153a006 CASWeb of Science®Google Scholar Goll, D.E. and Robson, R.M. 1967. Molecular properties of post-mortem muscle. 1. Myofibrillar nucleosidetrlphosphatase activity of bovine muscle. J. Food Sci. 32: 323. 10.1111/j.1365-2621.1967.tb01322_32_3.x CASWeb of Science®Google Scholar Goll, D.E., Arakawa, N., Stromer, M.H., Busch, W.A. and Robson, R.M. 1970. In " The Physiology and Biochemistry of Muscle as a Food," ed. E.J. Briskey, R.G. Cassens and B.B. Marsh vol. 2, p. 755. University of Wisconsin Press. Google Scholar Gothard, R.H., Mullins, A.M., Boulware, R.F. and Hansard, S.L. 1966. Histological studies of post-mortem changes in sarcomere length as related to bovine muscle tenderness. J. Food Sci. 31: 825. 10.1111/j.1365-2621.1966.tb03256.x Web of Science®Google Scholar Greaser, M.L., Cassens, R.G., Briskey, E.J. and Hoekstra, W.G. 1969. Post-mortem changes in subcellular fractions from normal and Pale, soft, exudative porcine muscle. 1. Calcium accumulation and adenosine tri-phosphatase activities. J. Food Sci. 34: 120. 10.1111/j.1365-2621.1969.tb00901.x CASWeb of Science®Google Scholar Haga, T., Maruyama, K. and Noda, H. 1965. Formation of actomyosin during the extraction of muscle mince with Weber-Edsall solution. Biochim. Biophys. Acta 94: 226. 10.1016/0926-6585(65)90027-0 CASPubMedWeb of Science®Google Scholar Haga, T., Yamamoto, M., Maruyama, K. and Noda, H. 1966. The effect of myosin and calcium on the solubilization of F-actin from muscle mince. Biochim. Biophys. Acta 127: 128. 10.1016/0304-4165(66)90483-1 CASPubMedWeb of Science®Google Scholar Herring, H.K., Cassens, R.G. and Briskey, E.J. 1969a. Studies on bovine natural actomyosin. 1. Relationship of ATPase and contractility to tenderness of muscle. J. Food Sci. 34: 389. 10.1111/j.1365-2621.1969.tb12785.x CASWeb of Science®Google Scholar Herring, H.K., Cassens, R.G., Fukazawa, T. and Briskey, E.J. 1969b. Studies on bovine natural actomyosln. 2. Physico-chemical properties and tenderness of muscle. J. Food Sci. 34: 571. 10.1111/j.1365-2621.1969.tb12092.x CASWeb of Science®Google Scholar Johnson, P. and Rowe, A.J. 1964. In " Biochemistry of Muscle Contraction," ed. J. Gergely, p. 279. Little, Brown, and Co., Boston . Google Scholar Khan, A.W. and Van den Berg, L. 1964. Changes in chicken muscle proteins during aseptic storage at above-freezing temperatures. J. Food Sci. 29: 49. 10.1111/j.1365-2621.1964.tb01692.x CASWeb of Science®Google Scholar Kielley, W.W. and Bradley, L.B. 1956. The relationship between sulfhydryl groups and the activation of myosin adenosine triphosphatase. J. Biol. Chem. 218: 653. CASPubMedWeb of Science®Google Scholar King, F.J. 1966. Ultracentrifugal analysis of changes in the composition of myofibrillar protein extracts obtained from fresh and frozen cod muscle. J. Food Sci. 31: 649. 10.1111/j.1365-2621.1966.tb01920.x CASWeb of Science®Google Scholar Koonz, C.H., Darrow, M.I. and Essary, E.O. 1954. Factors Influencing tenderness of principal muscles composing the poultry carcass. Food Tech. 8: 97. Web of Science®Google Scholar Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. 1951. Protein measurements with the Folin phenol reagent. J. Biol. Chem. 193: 265. 10.1016/S0021-9258(19)52451-6 CASPubMedWeb of Science®Google Scholar Maddox, C.E.R. and Perry S.V. 1966. Differences in the myosins of the red and white muscles of the pigeon. Biochem. J. 99: 8P. CASGoogle Scholar Mihalyi, E. and Rowe, A.J. 1966. Studies on the extraction of actomyosin from rabbit muscle. Biochem. Z. 345: 267. CASWeb of Science®Google Scholar Okitani, A., Arakawa, N. and Fujimaki, M. 1965. The changes of "Myosin B" during storage of rabbit muscle. 3. Sedimentation studies on "Myosin B." Agr. Biol. Chem. 29: 971. 10.1271/bbb1961.29.971 CASWeb of Science®Google Scholar Oyama, V.I. and Eagle, H. 1956. Measurements of cell growth in tissue culture with a phenol reagent (Folin-Ciocalteau). Proc. Soc. Exptl. Biol. Med. 91: 305. 10.3181/00379727-91-22245 CASPubMedWeb of Science®Google Scholar Penny, I.F. 1968. Effect of aging on the properties of myofibrils of rabbit muscle. J. Sci. Fd. Agric. 19: 518. 10.1002/jsfa.2740190908 CASWeb of Science®Google Scholar Perry, S.V. and Leadbetter, L. 1964. In " Biochemistry of Muscle Contraction." ed. J. Gergely p. 270. Little, Brown, and Co., Boston . Google Scholar Quass, D.W. and Brlskey, E.J. 1968. A study of certain properties of myosin from skeletal muscle. J. Food Sci. 33: 180. 10.1111/j.1365-2621.1968.tb01346.x CASWeb of Science®Google Scholar Robson, R.M., Goll, D.E. and Main, M.J. 1967. Molecular properties of post-mortem muscle. 5. Nucleoside triphosphatase activity of bovine myosin B. J. Food Sci. 32: 544. 10.1111/j.1365-2621.1967.tb00828.x CASWeb of Science®Google Scholar Schachman, H.K. 1957. In " Methods in Enzymology," ed. Colowick and Kaplan, Vol 4, p. 32. Academic Press. Inc.. Web of Science®Google Scholar Scharpf, L.G. Jr., Marion, W.W. and Forsythe, R.H. 1966. Post-rigor changes in selected physicochemical properties of myosin B fraction of turkey muscle. J. Food Sci. 31: 680. 10.1111/j.1365-2621.1966.tb01924.x Web of Science®Google Scholar Sedlak, J. and Lindsay, R.H. 1968. Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal. Biochem. 25: 192. 10.1016/0003-2697(68)90092-4 CASPubMedWeb of Science®Google Scholar Seidel, J.C. 1969. Similar effects on enzymic activity due to chemical modification of either of two sulfhydryl groups of myosin. Biochim. Biophys. Acta 180: 216. 10.1016/0005-2728(69)90215-1 CASPubMedWeb of Science®Google Scholar Seidel, J.C., Sreter, F.A., Thompson, M.M. and Gergely, J. 1964. Comparative studies of myofibrils, myosin and actomyosin from red and white rabbit skeletal muscle. Biochem. Biophys. Res. Commun. 17: 662. 10.1016/0006-291X(64)90411-5 CASWeb of Science®Google Scholar Stadelman, W.J. and Wise, R.G. 1961. Tenderness of poultry meat. 1. Effect of anesthesia, cooking, and irradiation. Food Technol. 15: 292. Web of Science®Google Scholar Sreter, F.A., Seidel, J.C. and Gergely, J. 1966. Studies on myosin from red and white skeletal muscles of the rabbit. 1. Adenosine triphosphatase activity. J. Biol. Chem. 241: 5772. CASPubMedWeb of Science®Google Scholar Stromer, M.H., Goll, D.E. and Roth, LE. 1967. Morphology of rigor-shortened bovine muscle and the effect of trypsin on pre- and post-rigor myofibrils. J. Cell Biol. 34: 431. 10.1083/jcb.34.2.431 PubMedWeb of Science®Google Scholar Takahashi; K., Fukazawa, T. and Yasui, T. 1967. Formation of myofibrillar fragments and reversible contraction of sarcomeres in chicken pectoral muscle. J. Food Sci. 32: 409. 10.1111/j.1365-2621.1967.tb09697.x Web of Science®Google Scholar Weber, H.H. 1950. Muskelproteine. Biochim. Biophys. Acta 4: 12. 10.1016/0006-3002(50)90004-7 CASPubMedWeb of Science®Google Scholar Wu, C.-S.C. 1969. Comparative studies on myosins from breast and leg muscles of chicken. Biochemistry 8: 39. 10.1021/bi00829a007 CASPubMedWeb of Science®Google Scholar Wu, C.S.C. and Sayre, R.N. 1971. Myosin stability in intact chicken muscle and a protein component released after aging. J. Food Sci. 36: 133. 10.1111/j.1365-2621.1971.tb02054.x CASWeb of Science®Google Scholar Yang, R., Okitani, A. and Fujimaki, M. 1970. Studies on myofibrils from the stored muscle. 1. Post-mortem chanaes in ATPase activity of myofibrils from rabbit muscle. Agric. Biol. Chem. 34: 1765. CASGoogle Scholar Citing Literature Volume37, Issue3May 1972Pages 346-350 ReferencesRelatedInformation

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