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- W2007592349 abstract "Abstract 1. 1. Crude muscle extracts, washed myofibrils and actins were isolated from frozen skeletal muscles of two hemoglobin-free fish—Chaenocephalus aceratus and Champsocephalus gunnari and of red-blooded antarctic Notothenia sp. 2. 2. SDS gel electrophoresis reveals some differences in a pattern of M line and regulatory proteins between white- and red-blooded fish, while actin of all the three species has the same mol.wt 43,000 D. 3. 3. A method conventionally used for fish myosin preparation was unsuccessful when applied to a frozen muscle of antarctic fish for this protein becomes very easily denaturated during storage and process of isolation. 4. 4. Patterns obtained upon electrophoresis in 8 M urea suggest that no differences in low molecular proteins of acidic nature exist between the investigated antarctic fish. Possible occurrence of parvalbumins in the isolated washed myofibrils is suggested." @default.
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- W2007592349 date "1981-01-01" @default.
- W2007592349 modified "2023-09-26" @default.
- W2007592349 title "Electrophoretic study of the myofibrillar proteins from white- and red-blooded antarctic fish" @default.
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- W2007592349 doi "https://doi.org/10.1016/0305-0491(81)90212-1" @default.
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