Journal
JOURNAL OF FOOD SCIENCE
Volume 71, Issue 3, Pages C196-C199Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2621.2006.tb15617.x
Keywords
oxidation; myosin; cross-linking; disulfide bond; chymotryptic digestion
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The cross-linking site(s) of myosin heavy chains (MHC) in chicken myofibrils exposed to non-enzymatic, hydroxyl radical-generation oxidizing systems (HRGS) was investigated by means of chymotryptic digestion and subsequent electrophoresis. Oxidation of the chymotryptic digests resulted in cross-linking of the rod or light meromyosin (LMM) segment of MHC mostly via disulfide bonds, while subfragment-1 (S-1) or heavy meromyosin (HMM) was not affected. A mixture of cross-linked rod or LMM and uncross-linked S-1 or HMM was also produced when myofibrils were 1st oxidized and then digested with chymotrypsin, confirming that cross-linking of myosin in HRGS-oxidized myofibrils occurred initially in the LMM portion of the myosin rod.
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