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Volumn 58, Issue 3, 2000, Pages 271-277

Conformational changes of myosin by gamma irradiation

Author keywords

Gamma irradiation; Myosin; Structural modification

Indexed keywords

BIOASSAY; CONFORMATIONS; ELECTROPHORESIS; ENZYMES; HYDROPHOBICITY; MOLECULAR WEIGHT; MUSCLE; RADIATION EFFECTS;

EID: 0034193392     PISSN: 0969806X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-806X(99)00466-1     Document Type: Article
Times cited : (32)

References (21)
  • 2
    • 0021131036 scopus 로고
    • Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress
    • Asghar A., Morita J., Samejima K., Yasui T. Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress. Agric. Biol. Chem. 48:1984;2217.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 2217
    • Asghar, A.1    Morita, J.2    Samejima, K.3    Yasui, T.4
  • 3
    • 0000827266 scopus 로고
    • Thermal aggregation of myosin subfragments from cod and herring
    • Chan J.K., Gill T.A., Paulson A.T. Thermal aggregation of myosin subfragments from cod and herring. J. Food Sci. 58:1993;1057.
    • (1993) J. Food Sci. , vol.58 , pp. 1057
    • Chan, J.K.1    Gill, T.A.2    Paulson, A.T.3
  • 4
    • 21844496982 scopus 로고
    • Quantification of beef myofibrillar proteins by SDS-PAGE
    • Claeys E., Buts U.R., Demeyer D. Quantification of beef myofibrillar proteins by SDS-PAGE. Meat Sci. [V]39:1995;177.
    • (1995) Meat Sci. , vol.539 , pp. 177
    • Claeys, E.1    Buts, U.R.2    Demeyer, D.3
  • 6
    • 0003707396 scopus 로고
    • N.W. Holm, & R.J. Berry. New York: Dekker
    • Holm N.W., Berry R.J. Manual on Radiation Dosimetry. 1970;Dekker, New York.
    • (1970) Manual on Radiation Dosimetry
  • 7
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • Horowits R., Kempner E.S., Bisher M.E., Podolsky R.J. A physiological role for titin and nebulin in skeletal muscle. Nature. 323:1986;160.
    • (1986) Nature , vol.323 , pp. 160
    • Horowits, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.J.4
  • 8
    • 0028998433 scopus 로고
    • Changes in structural and antigenic properties of proteins by radiation
    • Kume T., Matsuda T. Changes in structural and antigenic properties of proteins by radiation. Radiat. Phys. Chem. 46:1995;225.
    • (1995) Radiat. Phys. Chem. , vol.46 , pp. 225
    • Kume, T.1    Matsuda, T.2
  • 9
    • 0002569580 scopus 로고
    • Immunochemical identification of irradiated chicken eggs
    • Kume T., Ishii T., Matsuda T. Immunochemical identification of irradiated chicken eggs. J. Sci. Food Agric. 65:1994;1.
    • (1994) J. Sci. Food Agric. , vol.65 , pp. 1
    • Kume, T.1    Ishii, T.2    Matsuda, T.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of binding abilitycteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of binding abilitycteriophage T4. Nature. 227:1970;680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 11
    • 0032276171 scopus 로고    scopus 로고
    • Application of competitive indirect enzyme linked immunosorbent assay (Ci-ELISA) for monitoring the degree of frozen denaturation of bovine myosin
    • Lee J.W., Park J.H., Kim S.B., Kim C.J., Shin H.K. Application of competitive indirect enzyme linked immunosorbent assay (Ci-ELISA) for monitoring the degree of frozen denaturation of bovine myosin. Int. J. Food Sci. Technol. 33:1998;401.
    • (1998) Int. J. Food Sci. Technol. , vol.33 , pp. 401
    • Lee, J.W.1    Park, J.H.2    Kim, S.B.3    Kim, C.J.4    Shin, H.K.5
  • 12
    • 0032281316 scopus 로고    scopus 로고
    • Monitoring thermally induced conformational changes in bovine muscle myosin by competitive indirect enzyme linked immunosorben assay (CI-ELISA)
    • Lee J.W., Park J.H., Kim C.J., Shin H.K. Monitoring thermally induced conformational changes in bovine muscle myosin by competitive indirect enzyme linked immunosorben assay (CI-ELISA). Int. J. Food Sci. Technol. 33:1998;411.
    • (1998) Int. J. Food Sci. Technol. , vol.33 , pp. 411
    • Lee, J.W.1    Park, J.H.2    Kim, C.J.3    Shin, H.K.4
  • 13
    • 84985274569 scopus 로고
    • Heat-induced gelation of chicken gizzard myosin
    • Morita J., Sugayama H., Kondo K. Heat-induced gelation of chicken gizzard myosin. J. Food Sci. 59:1994;720.
    • (1994) J. Food Sci. , vol.59 , pp. 720
    • Morita, J.1    Sugayama, H.2    Kondo, K.3
  • 14
    • 21144466317 scopus 로고
    • Definition of optimum freezing rate - 2. Investigation of the physico-chemical properties of beef M. longissimus dorsi frozen at different freezing rates
    • Petrovic L., Grujic R., Petrovic M. Definition of optimum freezing rate - 2. Investigation of the physico-chemical properties of beef M. longissimus dorsi frozen at different freezing rates. Meat Sci. 33:1993;319.
    • (1993) Meat Sci. , vol.33 , pp. 319
    • Petrovic, L.1    Grujic, R.2    Petrovic, M.3
  • 16
    • 0001963373 scopus 로고
    • Wholesomeness of irradiated foods
    • Thayer D.W. Wholesomeness of irradiated foods. Food Technol. 48:1994;132.
    • (1994) Food Technol. , vol.48 , pp. 132
    • Thayer, D.W.1
  • 17
    • 0042486775 scopus 로고
    • A Simple fluorometric method for fat-binding capacity as an index of hydrophobicity of proteins
    • Tsutsui T., Li-chan E., Nakai S. A Simple fluorometric method for fat-binding capacity as an index of hydrophobicity of proteins. J. Food Sci. 51:1986;1268.
    • (1986) J. Food Sci. , vol.51 , pp. 1268
    • Tsutsui, T.1    Li-Chan, E.2    Nakai, S.3
  • 18
    • 85005583458 scopus 로고
    • Effect of frozen storage on protein denaturation in bovine muscle. I. Myofibrillar ATPase activity and differential sanning calorimetric studies
    • Wagner J.R., Añon M.C. Effect of frozen storage on protein denaturation in bovine muscle. I. Myofibrillar ATPase activity and differential sanning calorimetric studies. J. Food Technol. 21:1986;9.
    • (1986) J. Food Technol. , vol.21 , pp. 9
    • Wagner, J.R.1    Añon, M.C.2
  • 19
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • Weeds A.G., Pope B. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:1977;129.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129
    • Weeds, A.G.1    Pope, B.2
  • 20
    • 0000694043 scopus 로고
    • Thermal transitions in myosin-ANS fluorescence and gel rigidity
    • Wicker L., Lanier T.C., Hamann D.D., Akahane T. Thermal transitions in myosin-ANS fluorescence and gel rigidity. J. Food Sci. 51:1986;1540.
    • (1986) J. Food Sci. , vol.51 , pp. 1540
    • Wicker, L.1    Lanier, T.C.2    Hamann, D.D.3    Akahane, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.