Advanced SearchSearch Tips
Purification and Properties of Bovine Skeletal Muscle Proteasome
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Purification and Properties of Bovine Skeletal Muscle Proteasome
Yamamoto, S.; Gerelt, B.; Nishiumi, T.; Suzuki, A.;
  PDF(new window)
This paper describes the purification and properties of a multicatalytic proteinase complex, proteasome, from bovine skeletal muscle, in comparision with proteasome prepared from other species or organs. The purified bovine skeletal muscle proteasome exhibited a single band on polyacrylamide gel electrophoresis under nondenaturing conditions. Bovine skeletal muscle proteasome degraded synthetic peptides maximally at pH 8.0. Relative to pH 8.0, activities were gradually decreased with the lowering pH, but the extent of decrease was substrate-dependent, and the activity at pH 5.5 still retained 78-10% of the activity at pH 8.0, indicating the possibility that the proteasome is active in muscle during aging. When the proteasome was heated at 60 for 15 or 30 min and treated in the presence of 0.0125% SDS, the activity increased over 1.8 and 3.1 times (LLVY (Suc-Leu-Leu-Val-Tyr-NH-Mec) as a substrate), respectively. These results (activation with heat or SDS) indicate that the hydrolytic activity of proteasome was stimulated under mild denaturing conditions. The characteristics of the bovine skeletal muscle proteasome obtained in our experiment were almost the same as those of the proteasome prepared from other species or organs.
Bovine;Proteasome;SDS Treatment;Heat Treatment;Immunobloting;Meat Aging;
 Cited by
Stability of Proteasomes Extracted from Pressurized, Aged Skeletal Muscles,Yamamoto, Shuhei;Suzuki, Atsushi;Nishiumi, Tadayuki;

Asian-Australasian Journal of Animal Sciences, 2009. vol.22. 2, pp.282-288 crossref(new window)
Akashi, T., T. Shiomi, H. Sawada and H. Yokosawa. 1996. Purification and properties of the 26S proteasome from the rat brain: Evidence for its degradation of myelin basic protein in a ubiquitin-dependent manner. Brain Research 722:139-144.

Dahlmann, B., M. Rutschmann, L. Kuehn and H. Reinauer. 1985. Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acid or sodium dodecyl sulphate. Biochem. J. 228:171-177.

Davis, B. J. 1964. Disk electrophoresis-II. Method and application to human serum protein. Annals of the New York Academy of Sci. 121:404-427.

Gardrat, F., B. Fraigneau, V. Montel, J. Raymond and J. L. Azanza. 1999. Effect of high hydrostatic pressure on 20S proteasome activity. Eur. J. Biochem. 262:900-906.

Hoffman, L., C. Gorbea and M. Rechsteiner. 1999. Identification, molecular cloning, and characterization of subunit 11 of the human 26S proteasome. FEBS Lett. 449:88-92.

Kanayama, H., T. Tamura, S. Ugai, S. Kagawa, N. Tanahashi, T. Yoshimura, K. Tanaka and A. Ichihara. 1992. Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. Eur. J. Biochem. 206:567-578.

Kim, K., Y. Ikeuchi and A. Suzuki. 1995. Cleavage of connectin by calpain and cathepsin D. Biosci. Biotech. Biochem. 59:896-899.

Kimura, S. and K. Maruyama. 1989. Isolation of $\alpha$-connectin, an elastic protein, from rabbit skeletal muscle. J. Biochem. 106:952-954.

Koohmaraie, M. 1992. Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization and comparision of its effects on myofibrils with $\mu$-calpains. J. Anim. Sci. 70:3697-3708.

Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227:680-685.

Matsuishi, M. and A. Okitani. 1997. Proteasome from rabbit skeletal muscle: Some properties and effect on muscle proteins. Meat Sci. 45:451-462.

Mellgren, R. L. 1990. Interaction of human erythrocyte multicatalytic proteinase with polycations. Biochimica et Biophysica Acta. 995:181-186.

Mykles, D. L. 1989a. High-molecular-weight serine proteinase from lobster muscle that degrades myofibrillar proteins. J. Exp. Zool. 250:244-252. crossref(new window)

Mykles, D. L. 1989b. Purification and characterization of multicatalytic proteinase from crustacean muscle: comparison of latent and heat-activated forms. Arch. Biochem. Biophys. 274:216-228.

Mykles, D. L. and M. F. Haire. 1995. Branched-chain-amino-acidpreferring peptidase activity of the lobster multicatalytic proteinase (proteasome) and the degradation of myofibrillar proteins. Biochem. J. 306:285-291.

Orlowski, M. and S. Wilk. 1981. A multicatalytic proteinase complex from pituitary that froms enkephalin and enkephalin containing peptides. Biochem. Biophys. Res. Comm. 101:814-822.

Orlowski, M. 1990. The multicatalytic proteinase complex, a major extralysosomal proteolytic system. Biochemistry. 29:10289-10297.

Otsuka, Y., N. Homma, K. Shiga, J. Ushiki, Y. Ikeuchi and A. Suzuki. 1998. Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure. Meat Sci. 49:365-378.

Ouali, A. 1992. Proteolytic and physicochemical mechanisms involved in meat texture development. Biochinie. 74:251-265.

Rivett, A. J. 1989a. The multicatalytic proteinase of mammalian cells. Arch. Biochem. Biophys. 268:1-8.

Rivett, A. J. 1989b. The multicatalytic proteinase. J. Biolog. Chem. 264:12215-12219.

Rivett, A. J. 1993. Proteasome: multicatalytic proteinase complexs. Biochem. J. 291:1-10.

Robert, N., M. Briand, R. Taylor and Y. Briand. 1999. The effect of proteasome on myofibrillar structures in bovine skeletal muscle. Meat Sci. 51:149-153.

Sentandreu, M. A., G. Coulis and A. Ouali. 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci. Tech. 13:398-419.

Tanaka, K., K. Ii, A. Ichihara, L. Waxman and A. L. Goldberg. 1986. A high molecular weight proteinase in the cytosol of rat liver. J. Biol. Chem. 261:15197-15203.

Taylor, R. G., C. Tassy, M. Briand, N. Robert, Y. Briand and A. Ouali. 1995. Proteolytic activity of proteinase on myofibrillar structure. Mol. Biol. Rep. 21:71-73.

Towbin, H., T. Staehelin and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheet: Procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.

Trinick, J., P. Knight and A. Whiting. 1984. Purification and properties of native titin. J. Mol. Biol. 180:331-356.

Wagner, B. J. and J. W. Margolis. 1993. Thermal stability and activation of bovine lens multicatalytic proteinase complex (proteasome). Arch. Biochem. Biophys. 307:146-152.

Wilk, S. and M. Orlowski. 1983. Evidence that pituitary cationsensitive neutral endopeptidase is a multicatalytic proteinase complex. J. Neurochem. 40:842-849.