カルパインで処理した変性ミオシンの存在様式

概要

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Filamentous carp myosin was incubated at 29°C with or without calpain in the medium containing 0.05M NaCI and 5mm Ca2+ at neutral pH. After the incubation both myosins were solubilized with either SDS, 4M urea or 0.6M NaCl, and then applied on gel filtration chromatography using agarose gel to analyze the mode of existence of the myosins.In the presence of SDS, the incubated myosin without calpain as well as native one was fully dissociated into its subunits, heavy and light chains, whereas calpain digested myosin existed as a mixture of Mr=150, 000 (150k) fragment and many other small fragments derived from myosin head portion, S-1.In the presence of 4M urea, it was shown that myosin heavy chain and light chains were dissociated from each other but existed independently in their aggregated forms. The 150k fragment also existed in its aggregated form.In the presence of 0.6M NaCl, the incubated myosins regardless of, with or without calpain were eluted from the gel column as a single peak at the void volume. It was, therefore, indicated that all myosin fragments, 150k and S-1 fragments, produced by calpain digestion existed in a form of noncovalently associated aggregate rather than a mixture of the fragments in the medium at physiological and higher salt concentrations.
日本水産學會の論文