Natural Actin and Tropomyosin from Molluscan Catch Muscle
Girich UV, Lazarev SS, Vyatchin IG, Matusovsky OS and Sheludko NS*
Laboratory of Cell Biophysics, A.V. Zhirmunsky Institute of Marine Biology, National Scientific Center of Marine Biology, Far Eastern Branch of the Russian Academy of Sciences, 17 Palchevsky Str., ladivostok 690041, Russia
- *Corresponding Author:
- Sheludko NS
Laboratory of Cell Biophysics, A.V. Zhirmunsky
Institute of Marine Biology, National Scientific
Center of Marine Biology, Far Eastern Branch
of the Russian Academy of Sciences
17 Palchevsky Str., Vladivostok 690041, Russia
E-mail: [email protected]
Received Date: June 12, 2017 Accepted Date: June 16, 2017 Published Date: June 22, 2017
Citation: Girich UV, Lazarev SS, Vyatchin IG, Matusovsky OS, Sheludko NS (2017) Natural Actin and Tropomyosin from Molluscan Catch Muscle. J Phys Chem Biophys 7: 249. doi: 10.4172/2161-0398.1000249
Copyright: © 2017 Girich UV, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
In this work, the main proteins of thin filaments (actin and tropomyosin) were isolated from the catch muscle of the mussel Crenomytilus grayanus and the rabbit skeletal muscles. Rabbit actin and tropomyosin and mussel tropomyosin were isolated by traditional methods as opposed to "natural" mussel actin (isolation of the mussel actin from acetone powder is impossible). These proteins were used to reconstruct actin+tropomyosin complexes in nonhybrid and hybrid manner. A non-hybrid complex, reconstructed from rabbit actin and tropomyosin, has higher reduced viscosity than complex of mussel proteins where reduced viscosity was nearly indistinguishable from the intrinsic viscosity. ÐÂoth rabbit and mussel actin were purified by polymerization-repolymerization cycles followed by gel filtration chromatography. During purification, the viscosity of both actins increased, and the difference in viscosity between them decreased. Based on the SDS-electrophoresis, we did not find any of the other proteins in the chromatographic fractions, except actin. However, obtained chromatographic fractions have significant differences in viscosity and rate of polymerization. We believe that these properties caused by the presence of an "ending factor” (such as β-actinin or Cap Z) in actin preparations. The data obtained indicate that isolation of “natural” actin is accompanied by a coextraction of an unknown or known "ending factor" in amounts that may be greater than those obtained from the acetone powder of rabbit skeletal muscles.