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DIFFERENCE IN Z‐LINE REMOVAL BETWEEN NORMAL AND PSE PORCINE MYOFIBRILS
Author(s) -
KANG C. G.,
MUGURUMA M.,
FUKAZAWA T.,
ITO T.
Publication year - 1978
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.1365-2621.1978.tb02341.x
Subject(s) - myofibril , chemistry , trypsin , fragmentation (computing) , sodium , protease , chromatography , biochemistry , enzyme , biology , ecology , organic chemistry
Z‐line removal from isolated myofibrils of normal and PSE porcine muscles by a Ca 2+ ‐activated protease (CAF) and trypsin was investigated. Z‐line substances were also extracted from normal and PSE myofibrils with sodium desoxycholate. Z‐line removal by CAF or trypsin digestion which accompanies fragmentation and release of soluble materials from myofibrils was much less for PSE myofibril than for normal. During the digestion reaction with CAF, α‐actinin and troponin‐T were specifically degradated. α‐actinin was also extracted from myofibrils with sodium desoxycholate. The interrelationship between the extractability of α‐actinin with sodium desoxycholate and the difficulty of fragmentation of PSE myofibrils is discussed.