ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Changes in biochemical properties of myofibrillar proteins of rabbit muscle, which had been subjected to electrical stimulation soon after slaughter, during postmortem storage at 0°C were investigated. Myofibrillar ATPase activity and the ATPase activity of acto-heavy meromyosin (HMM) complex, reconstituted from actin and HMM which had been prepared from at-death and postmortem muscles, decreased at first and then increased slightly during 7 days storage. In addition, the change of the dissociation constant of acto-HMM complex of electrically stimulated muscle during postmortem storage was quite small, i.e., 1.59 ± 10−4M for at-death muscle, 1.70 ± 10−4M for muscle stored for 1 day and 1.49 ± 10−4M for muscle stored for 7 days. This indicates that electrical stimulation treatment minimized the postmortem change of actin-myosin interaction.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1983.tb14779.x
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