魚類筋肉トロポニンの性質の比較について

概要

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Troponins were extracted from the myofibrils of white lateral muscles of six species of fishes with low ionic strength solution. They were partially purified by salting out with ammonium sulfate and separated from tropomyosin at pH 4.5 in 0.4M LiCl. Most of the preparations showed four major protein bands on sodium dodecyl sulfate polyacrylamide gel electrophoretograms. Two components with molecular weights of 30, 000 and 43, 000 were found in all of the preparations. The 43, 000 component was removed from the preparations by DEAE-cellulose chromatography. The other two components having lower molecular weights differed in size with fish species. Each of carp, big eye tuna, tilapia, rainbow trout, and mackerel troponins formed a functional complex with carp tropomyosin and conferred full calcium sensitivity on Mg2+-ATPase of desensitized carp actomyosin. Carp tropomyosin could replace the other fish tropomyosin. This lack of species specificity provides evidence for the essential similarity of the regulatory proteins in teleost muscles.
日本水産學會の論文