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Isolation of Actomyosin and Myosin from Post‐Rigor Turkey Breast and Thigh
Author(s) -
DUDZIAK JUDITH A.,
FOEGEDING E. ALLEN
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb09258.x
Subject(s) - myosin , actin , myosin light chain kinase , size exclusion chromatography , chemistry , electrophoresis , anatomy , biochemistry , biology , enzyme
Myosin/actomyosin (MAM) was extracted from post‐rigor turkey breast and thigh muscles using Hasselbach‐Schneider solution. Electrophoretic evaluation of the breast muscle protein extract showed it to be 86.4% myosin and 7% actin. Thigh muscle MAM contained 79.4% myosin and 4.7% actin. Slight variations in minor protein bands were observed between the breast and thigh MAM electrophoretic profiles. Gel filtration of MAM on a 2% agarose column separated actomyosin from myosin. Myosin purity was 97.9% and 99.2% for breast and thigh, respectively. Gel filtration data indicated that myosin, unassociated with actin, was the predominate protein extracted from the post‐rigor tissue. Myosin was approximately 67‐72% of the original MAM.