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- W1982971386 abstract "Abstract 1. 1. Two out of three light chains of myosin from mixed hind leg muscles of the frog (LC 1 and LC 2 ) undergo a proteolytic cleavage during preparation with procedures routinely used to obtain myosin from skeletal muscles of other vertebrates. 2. 2. The intact LC 1 and LC 3 comigrate on SDS-polyacrylamide gels with the respective light chains of rabbit fast skeletal muscle; LC 2 has lower mobility than the rabbit LC 2 . All the three light chains differ from their counterparts in the rabbit myosin in mobilities on urea-polyacrylamide gels. 3. 3. The LC 2 of frog myosin is released upon DTNB-EDTA † treatment more easily than LC 2 of rabbit fast skeletal muscle. 4. 4. Differences in the fragmentation of the heavy chains of myosin from hind leg and from rabbit fast skeletal muscles by trypsin indicate some differences in primary and/or secondary structure. 5. 5. Fast inactivation accompanied by aggregation of frog myosin was confirmed. Pyrophosphate was shown to have a protective effect. 6. 6. Myosin from mixed hind leg muscles of the frog is similar to myosin from rabbit slow skeletal muscle in its instability under mild alkaline conditions." @default.
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- W1982971386 date "1979-01-01" @default.
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- W1982971386 title "Subunit composition and some other properties of myosin from skeletal muscles of the frog rana esculenta" @default.
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