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A. Chakravorty, B. Biswas (1965)
Nonterminal incorporation of guanosine monophosphate from guanosine triphosphate by an enzyme system from spinach chloroplasts.The Journal of biological chemistry, 240 11
O. Lowry, N. Rosebrough, A. Farr, R. Randall (1951)
Protein measurement with the Folin phenol reagent.The Journal of biological chemistry, 193 1
J. Acton, R. Saffle (1972)
EMULSIFYING CAPACITY OF MUSCLE PROTEIN: PHASE VOLUMES AT EMULSION COLLAPSEJournal of Food Science, 37
S. Galluzzo, J. Regenstein (1978)
ROLE OF CHICKEN BREAST MUSCLE PROTEINS IN MEAT EMULSION FORMATION: MYOSIN, ACTIN AND SYNTHETIC ACTOMYOSINJournal of Food Science, 43
J. Potter (1974)
The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils.Archives of biochemistry and biophysics, 162 2
J. Spudich, S. Watt (1971)
The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.The Journal of biological chemistry, 246 15
S. Galluzzo, J. Regenstein (1978)
EMULSION CAPACITY AND TIMED EMULSIFICATION OF CHICKEN BREAST MUSCLE MYOSINJournal of Food Science, 43
Weber Weber, Olson Olson (1969)
The reliability of molecular weight determination by dodecyl‐sulfate polyacrylamide gel electrophoresisJ. Biol. Chem., 240
ABSTRACT Natural actomyosin (NAM) and glycerinated myofibrils (contracted and uncontracted) from chicken breast muscle were taken to 0.6M NaCl, 20 mM citrate‐phosphate buffer (pH 7), and tested for emulsifying capacity (E.C.) and timed emulsification. Myofibrils were extracted for 0, 1, and 24 hr in the buffer prior to testing. The aqueous phase was separated by centrifugation and analyzed quantitatively by SDS gel electrophoresis. The E.C. of NAM was lower than that reported earlier for myosin, but was equal to it with added ATP or pyrophosphate. The E.C. of myofibrils varied considerably depending upon whether the 0.6M NaCl soluble protein or the initial protein concentration was used as the denominator. Timed emulsification studies showed that actomyosin was removed from solution in a manner similar to myosin alone. However, when this complex was dissociated, actin remained in the aqueous phase, while myosin was preferentially used in the emulsion. The same relationship was displayed in myofibrils. The regulatory proteins tropomyosin and troponin exhibited a behavior independent of both actin and myosin. Tropomyosin always increased in the aqueous phase relative to myosin regardless of the presence or absence of ATP, while the troponins were more readily removed from solution in the presence of ATP.
Journal of Food Science – Wiley
Published: Nov 1, 1978
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