Premium
A Study of Certain Properties of Myosin from Skeletal Muscle
Author(s) -
QUASS D. W.,
BRISKEY E. J.
Publication year - 1968
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.1365-2621.1968.tb01346.x
Subject(s) - myosin , skeletal muscle , sephadex , atpase , chemistry , myosin atpase , biochemistry , enzyme , biology , anatomy
SUMMARY— This investigation was conducted (a) to establish a procedure for purifying a stable myosin preparation from pig skeletal muscle and (b) to evaluate the enzymatic activity and associated characteristics of purified myosin, isolated at death from skeletal muscles which ultimately have varying rates of hydrolysis of ATP in situ during the first half‐hour after death. Rabbit muscles were also used for comparative purposes. Myosin preparations were found to be pure (by ultracentrifugation, Sephadex separation and superprecipitation tests) and stable with normal values for SH groups. The Ca ++ ‐activated ATPase activities of myosin extracted from PSE Poland China pigs were significantly greater than those from Chester White pigs and normal Poland China pigs. EDTA‐activated ATPase activities were greater in myosin from PSE Poland China than in normal Poland China.