Purification and characterization of a soluble methionyl aminopeptidase from porcine skeletal muscle

Meat Science

Volumn 56, Issue 3, 2000, Pages 247-254

  Flores, Mónica ^a   Marina, Miguel ^a   Toldrá, Fidel ^a  

^a INSTITUTO DE AGROQUÍMICA Y TECNOLOGÍA DE ALIMENTOS CSIC   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0034389147     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(00)00049-8     Document Type: Article

References (32)

1. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
2. Flores, J., & Toldrá, F. (1993). Curing: processes and applications. In R. Macrae, R. Robinson, M. Sadler, & G. Fullerlove, Encyclopaedia of food science, food technology and nutrition (pp. 1277-1282). London: Academic Press.
3. Flores M., Aristoy M.C., Toldrá F. HPLC purification and characterization of porcine muscle aminopeptidase B. Biochimie. 75:1993;861-867.
4. Flores M., Aristoy M.C., Toldrá F. HPLC purification and characterization of soluble alanyl aminopeptidase from porcine skeletal muscle. Journal of Agriculture and Food Chemistry. 44:1996;2578-2583.
5. Flores M., Aristoy M.C., Toldrá F. Curing agents affect aminopeptidase activity from porcine skeletal muscle. Zeitschrift für Lebensmittel Untersuchung und Forschung A. 205:1997;343-346.
6. Flores M., Aristoy M.C., Toldrá F. Feedback inhibition of porcine muscle alanyl and arginyl aminopeptidases in cured meat products. Journal of Agriculture and Food Chemistry. 46:1998;4982-4986.
7. Freitas J.O., Termignoni C., Guimaraes J.A. Microsomal methionine aminopeptidase. properties of the detergent-solubilized enzyme International Journal of Biochemistry. 17:1985;1285-1291.
8. Kato, H., Rhue, M. R., & Nishimura, T. (1989). Role of free amino acids and peptides in food taste. In R. Teranishi, R.G. Buttery, F. Shahidi, Flavor chemistry. Trends and development (pp. 158-174). ACS Symposium Series 388, Washington: ACS.
9. Kirschke H., Barrett A.J. Chemistry of lysosomal proteases. Glaumann H., Ballard F.J. Lysosomes: their role in protein breakdown. 1987;193-238 Academic Press, London.
10. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
11. Lauffart B., Mantle D. Rationalization of aminopeptidase activities in human skeletal muscle soluble extract. Biochimistry Biophysics Acta. 956:1988;300-306.
12. Ledeme N., Vincent-Fiquet O., Hennon G., Plaquet R. Human liver L-leucine aminopeptidase. evidence for two forms compared to pig liver enzyme Biochimie. 65:1983;397-404.
13. Mantle D., Lauffart B., McDermott J., Gibson A. Characterization of aminopeptidases in human kidney soluble fraction. Clinica Chimica Acta. 187:1990;105-114.
14. Mantle D., Lauffart B., Gibson A. Purification and characterization of leucyl aminopeptidase and pyroglutamyl aminopeptidase from human skeletal muscle. Clinina Chimica Acta. 197:1991;35-46.
15. McDonald J.K., Barret A.J. Mammaliam proteases: a glossary and bibliography. Vol 2., exopeptidases. 1986;Academic Press, London.
16. Merril, C. R., Goldman, D., Sedman, S. A., & Ebert, M. H. (1981). Ultra sensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid. Science, 211, 1437-1438.
17. Nishimura, T., Okitani, A., & Kato, H. (1988). Identification of Neutral Aminopeptidases Responsible for Peptidolysis in Post-mortem Rabbit Skeletal Muscle. Agricultural Biological Chemistry, 52, 2183-2190.
18. Nishimura, T., Okitani, A., Rhue, M. R., & Kato, H. (1990). Survey of Neutral Aminopeptidase in Bovine, Porcine, and Chicken Skeletal Muscles. Agricultural Biological Chemistry, 54, 2769-2775.
19. Nishimura T., Rhyu M.R., Kato H. Purification and properties of aminopeptidase H from porcine skeletal muscle. Agricultural Biological Chemistry. 55:1991;1779-1786.
20. Nishimura T., Rhyu M.R., Kato H., Arai S. Purification and properties of aminopeptidase H from bovine skeletal muscle. Journal of Agriculture and Food Chemistry. 42:1994;2709-2712.
21. Okitani A., Nishimura T., Kato H. Characterization of hydrolase H, a new muscle protease possesing aminoendopeptidase activity. European Journal of Biochemistry. 115:1981;269-274.
22. Okitani A., Nishimura T., Otsuka Y., Matsukura U., Kato H. Purification and properties of BANA hydrolase H of rabbit skeletal muscle, a new enzyme hydrolyzing α-N-Benzoyl-arginine-β-naphthylamide. Agricultural Biological Chemistry. 44:1980;1705-1708.
23. Rhyu M.R., Nishimura T., Kato Y., Okitani A., Kato H. Purification and properties of aminopeptidase H from chicken skeletal muscle. European Journal of Biochemistry. 208:1992;53-59.
24. Rothe M., Dodt J. Studies on the aminopeptidase activity of rat cathepsin H. European Journal of Biochemistry. 210:1992;759-764.
25. Singh H., Kalnitsky G. Separation of a new α-N-Benzoylarginine-β-naphthylamide hydrolase from Cathepsin B1. Journal of Biological Chemistry. 253:1978;4319-4326.
26. Singh H., Kalnitsky G. α-N-Benzoylarginine-β-naphthylamide hydrolase, an aminoendopeptidase from rabbit lung. Journal of Biological Chemistry. 255:1980;369-374.
27. Taylor A. Aminopeptidases. structure and function FASEB Journal. 7:1993;290-298.
28. Taylor A. Aminopeptidases. towards a mechanism of action TIBS. 18:1993;167-171.
29. Toldrá F., Flores M., Aristoy M.C. Enzyme generation of free amino acids and its nutritional significance in processed pork meats. Charalambous G. Food flavors: generation analysis and process influence. 1995;1303-1322 Elsevier Science Publishers, Amsterdam.
30. Toldrá F., Falkous G., Flores M., Mantle D. Comparison of aminopeptidase inhibition by amino acids in human and porcine skeletal muscle tissues in vitro. Comparative Biochemistry and Physiology. 115B:1996;445-450.
31. Toldrá F., Flores M. The role of muscle proteases and lipases in flavour development during the processing of dry-cured ham. Critical Reviews in Food Science and Nutrition. 38:1998;331-352.
32. Toldrá F. Proteolysis and lipolysis in flavour development of dry-cured meat products. Meat Science. 49:1998;S101-S110.