Characterization of peptides released from rabbit skeletal muscle troponin-T by μ-calpain under conditions of low temperature and high ionic strength

Meat Science

Volumn 59, Issue 1, 2001, Pages 61-69

  Hughes, M C ^a   Geary, S ^b   Dransfield, E ^c   McSweeney, P L H ^a   O'Neill, E E ^a  

^a Dept Food Sci Food Technol N   (Ireland)

^b UNIVERSITY COLLEGE CORK   (Ireland)

^c CEMAGREF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ORYCTOLAGUS CUNICULUS; VISCUM ALBUM;

EID: 0035609543     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(01)00052-3     Document Type: Article

References (36)

1. Carafoli, E., & Molinari, M. (1998). Calpain: a protein in search of a function? Biochemical and Biophysical Research Communications, 247, 193-203.
2. Clarke F.M., Lovell S.J., Masters C.J., Winzor D.J. Beef muscle troponin. evidence for multiple forms of troponin-T Biochimica et Biophysica Acta. 427:1976;617-626.
3. Croall D.E., DeMartino G.N. Calcium activated neutral protease (calpain) system. structure, function, and regulation Physiological Reviews. 71:1991;813-847.
4. Dabrowska R., Barylko B., Nowak E., Drabikowski W. The origin of 30,000 Dalton protein in troponin preparations. FEBS Letters. 29:1973;239-242.
5. Dransfield E. Modelling post-mortem tenderisation - IV. role of calpains and calpastatin in conditioning Meat Science. 34:1993;217-234.
6. Elgasim E.A., Koohmaraie M., Anglemier A.F., Kennick W.H., Elkhalifa E.A. The combined effects of the calcium activated factor and cathepsin D on skeletal muscle. Food Microstructure. 4:1985;51-61.
7. Goll D.E., Kleese W.C., Szpacenko A. Skeletal muscle proteases and protein turnover. Campion D.R., Hausman G.J., Martin R.J. Animal growth regulation. 1989;141-182 Plenum Publishers, New York.
8. +2 dependent proteinase. In B. DeBernard, G. L. Sottocasa, G. Sandri, E. Carafoli, A. N. Taylor, T. C. Vanaman, & R. I. P. Williams, Calcium-binding proteins(pp.19-35). Amsterdam: Elsevier.
9. Goll D.E., Thompson V.F., Taylor R.G., Christiansen J.A. Role of the calpain system in muscle growth. Biochimie. 74:1992;225-237.
10. Ho C.Y., Stromer M.H., Robson R.M. Identification of the 30 kDa polypeptide in post-mortem skeletal muscle as a degradation product of troponin-T. Biochimie. 76:1994;369-375.
11. Huff-Lonergan, E., Parrish, Jr. F. C., Olson, D. G. & Robson, R. M. (1995). Degradation of muscle structural proteins by μ-calpain under conditions simulating post-mortem pH, temperature and ionic strength, In Proceedings of 41st International Congress on Meat Science and Technology. San Antonio, USA.
12. Huff-Lonergan E., Mitsuhashi T., Beekman D.D., Parrish F.C. Jr., Olson D.G., Robson R.M. Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in post-mortem bovine muscle. Journal of Animal Science. 74:1996;993-1008.
13. Hughes M.C., O'Neill E.E., McSweeney P.L.H., Healy A. Proteolysis of bovine F-actin by cathepsin B. Food Chemistry. 64:1999;525-530.
14. Koohmaraie M. Role of the neutral proteinases in post-mortem muscle protein degradation and meat tenderness. Reciprocal Meat Conference Proceedings. 45:1992;63-74.
15. 2+ dependent proteases (calpains) in post-mortem proteolysis and meat tenderness. Biochimie. 74:1992;239-245.
16. Koohmaraie M., Schollmeyer J.E., Dutson T.R. Effect of low-calcium-requiring activated factor on myofibrils under varying pH and temperature conditions. Journal of Food Science. 51:1986;28-32.
17. Koohmaraie M., Whipple G., Kretchmar D.H., Crouse J.D., Mersmann H.J. Post-mortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. Journal of Animal Science. 69:1991;617-624.
18. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London). 227:1970;680-685.
19. Leszyk J., Dumaswala R., Potter J.D., Gusev N.B., Verin A.D., Tobacman L.S., Collins J.H. Bovine cardiac troponin-T. Amino acid sequences of the two isoforms Biochemistry. 26:1987;7035-7042.
20. Lowry O.H., Rosenbrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin reagent. Journal of Biological Chemistry. 193:1951;265-275.
21. 2+ dependent neutral proteinase. Biochimica et Biophysica Acta. 788:1984;11-16.
22. Negishi H., Yamamoto E., Kuwata T. The origin of the 30 kDa component appearing during post-mortem aging of bovine muscle. Meat Science. 42:1996;289-303.
23. Negishi H., Yamamoto E., Kuwata T. Separation and amino acid composition of three troponin components from bovine muscle. Meat Science. 42:1996;431-442.
24. Ohtsuki I. Molecular arrangement of troponin-T in the thin filament. Journal of Biochemistry. 86:1979;491-497.
25. Ohtsuki I., Shiraishi F., Suenaga N., Miyata T., Tanokura M. A 26 k fragment of troponin T from rabbit skeletal muscle. Journal of Biochemistry. 95:1984;1337-1342.
26. Olson D.G., Parrish F.C. Jr., Dayton W.R., Goll D.E. Effect of post-mortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle. Journal of Food Science. 42:1977;117-124.
27. Penny I.F., Dransfield E. Relationship between toughness and troponin-T in conditioned beef. Meat Science. 3:1979;135-141.
28. Risnik V.V., Verin A.D., Gusev N.B. Comparison of two cardiac troponin-T isoforms. Biochemical Journal. 225:1985;549-552.
29. Sasaki T., Kikuchi T., Yumoto N., Yoshimura N., Murachi T. Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. Journal of Biological Chemistry. 259:1984;12489-12494.
30. Samejima K., Wolfe F.H. Degradation of myofibrillar protein components during post-mortem aging of chicken muscle. Journal of Food Science. 41:1976;250-254.
31. Squire J. Thin filament structure and regulation. Squire J. The structural basis of muscular contraction. 1981;157-223 Plenum Press, London.
32. Takahashi K. Calpain substrate specificity. Mellgren R.L., Murachi T. Intracellular calcium-dependent proteolysis. 1990;55-74 CRC Press, USA.
33. Troy, D. J., Patyaryas, T., Tsitsilonis, O. E., Yialouris, P. P., Vazeou, S., Healy, A., Stoeva, S. & Voelter, W. (1997). Sequence analysis of proteins extracted from bovine myofibrillar extracts during the aging period. In Proceedings 43rd International Congress on Meat Science and Technology. Auckland, New Zealand.
34. Whipple G., Koohmaraie M. Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on post-mortem proteolysis. Journal of Animal Science. 70:1992;798-804.
35. Yates L.D., Dutson T.R., Caldwell J., Carpenter Z.L. Effect of temperature and pH on the post-mortem degradation of myofibrillar proteins. Meat Science. 9:1983;157-179.
36. Zeece M.G., Robson R.M., Lusby M.L., Parrish F.C. Jr. Effect of calcium activated protease (CAF) on bovine myofibrils under different conditions of pH and temperature. Journal of Food Science. 51:1986;797-803.