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Provedor de dados:  OceanDocs
País:  Belgium
Título:  Purificación de isoformas de proteasas tipo tripsina de crustáceos
Autores:  Rodríguez-Casariego, J.
Perdomo-Morales, R.
Perera, E.
Data:  2012-12-12
Ano:  2012
Palavras-chave:  Crustaceans
Resumo:  Las tripsinas son las principales peptidasas digestivas de crustáceos. En los últimos años se han producido revisiones sobre las tripsinas de invertebrados, así como de crustáceos, e incluso de las presentes en determinada especie de crustáceo. Sin embargo, los aspectos relacionados con la purificación de estas enzimas (y sus isoformas) no se han abordado en estas revisiones. En la presente revisión se exponen los procedimientos más empleados en la purificación de tripsinas de crustáceos, las dificultades en la separación de isoformas, y se discuten las experiencias de los autores en la purificación de isoformas de tripsina en la langosta espinosa Panulirus argus, las cuales pudieran ser de interés para los que se inicien en el campo de la purificación de enzimas tipo tripsina de crustáceos. Se excluyen los aspectos básicos relacionados con los principios de cada método y con la purificación de proteínas en general, los cuales pueden ser encontrados en la vasta literatura publicada tanto en revisiones como en libros especializados.

Trypsins are the main digestive proteinases in crustaceans. Some reviews have been published on the trypsin enzymes in invertebrates and particularly for crustaceans only few species have been analyzed. However, these reviews have not included the purification of the enzymes and their isoforms. The most employed procedures for the purification of crustacean trypsins are appraised in the present work, as well as the difficulties to separate the different isoforms. We discuss our own experience on the purification of the spiny lobster Panulirus argus trypsins. Aspects related with the principles of each method and the purification of proteins in general were omitted since they can be found in many published reviews and books.
Tipo:  Journal Contribution
Idioma:  Espanhol
Identificador:  Revista de Investigaciones Marinas, 32 (1), p. 1-8

1991-6086

http://hdl.handle.net/1834/4535
Relação:  Ahsan, M.M., Watabe, S (2001) Kinetic and structural properties of two isoforms of trypsin isolated from the viscera of Japanese anchovy, Engraulis japonicus. J. Protein. Chem. 20(1): 49-58. Amin, E., Saboury, A.A., Mansouri-Torshizi, H., Zolghadri, S., Bordbar, A.K. (2010) Evalua- tion of p-phenylene-bis and phenyl dithiocarbamate sodium salts as inhibitors of mushroom tyrosinase. Acta Biochem. Pol. 57(3): 277–283. Barret, A., Rawlings, N., Woessner, J. (1998) Handbook of proteolytic enzymes (2nd Ed.) Academic Press, San Diego. 1666 pp. Brockeroff, H., Hoyle, R.J., Hwang, P.C. (1970) Digestive enzymes of the American lobster (Homarus americanus). J. Fish. Res. Bd. Canada. 27, 1357-1370. Carrillo, O., Forrellat-Barrios, A., Guerrero-Galván, S., Vega-Villasante, F. (2007) A review of digestive enzyme activity in penaeid shrimps. Crustaceana 80, 257-275. Cereghino, G.P., Cereghino, J.L., Ilgen, C., Cregg, J.M. (2002) Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr. Op. Biotech. 13, 329- 332. Dechavanne, V., Barrillat, N., Borlat, F., Hermant, A., Magnenat, L., Paquet, M., Antonsson, B., Chevalet, L. (2011) A high-throughput protein refolding screen in 96-well format combined with design of experiments to optimize the refolding conditions. Protein Expression and Purification 75, 192–203. Dendinger, J.E., O'Connor, K.L. (1990) Purification and characterization of a trypsin-like enzyme from the midgut gland of the Atlantic blue crab, Callinectes sapidus. Comp. Biochem. Physiol. 95B (3), 525-530. Díaz, M., Ortego, F., García de Lacoba, M., Magaña, C., de la Poza, M., Farinós, G.P., Castañera, P., Hernández-Crespo, P. (2005) Diversity of trypsins in the Mediterranean corn borer Sesamia nonagrioides (Lepidoptera: Noctuidae), revealed by nucleic acid sequences and enzyme purification. Insect Biochem. Mol. Biol. 35, 1005–1020. Escamilla-Treviño, Y., Viader-Salvadó, J.M., Van- Wormhoudt, A., Sepúlveda-Saavedra, J., Leal-Gonzáles, R.M., Guerrero-Olazarán, M.G. (1999) Expression studies of shrimp trypsin and trypsinogen in Pichia pastoris. Current Topics in Gene Expression Systems- Meeting. Invitrogen Corporation and Reasearch Corporation Technologies, San Diego, California (U.S.A.). Figarella, C., Negri, G.A., Guy, O. (1975) The two human trypsinogens. Inhibition spectra of the two human trypsins derived from their purified zymogens. Eur. J. Biochem. 53, 457- 463. Fodor, K., Harmat, V., Hetényi, C., Kardos, J., Antal, J., Perczel, A., Patthy, A., Katona, G., Gráf, L. (2005) Extended intermolecular interac- tions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition. J Mol. Biol. 350, 156-169. Fu, X., Xue, C., Miao, B., Li, Z., Yang, W., Wang, B. (2005) Study of a highly alkaline protease extracted from digestive tract of sea cucumber (Stichopus japonicus). Food Research International 38, 323-329. Galgani, F., Nagayama, F. (1987) Digestive prote- inases in the Japanese spiny lobster Panulirus japonicus. Comp. Biochem. Physiol. 87B, 889–893. Gevaert, K., Vandekerckhove, J. (2000) Protein identification methods in proteomics. Electrophoresis 21, 1145-1154. Guerrero-Olazarán, M.G., Escamilla-Treviño, Y., Van-Wormhoudt, A., Sepúlveda- Saavedra, J., Viader-Salvadó, J.M. (2001) Efecto de la expresión en Pichia pastoris de una serinoproteasa sobre enzimas peroxisomales. Ciencia UANL 4(4): 448-453. Guizani, N., Marshall, M.R., Wei, C.I. (1992) Purification and characterization of a trypsin-like enzyme from the hepatopancreas of crayfish (Procambarus clarkii). Comp. Biochem. Physiol. 103B (4), 809-815. Hedstrom, L., (1996) Trypsin: A case study in the structural determinants of enzyme specificity. Biol. Chem. 377, 465-470. Hehemann, J.H., Redecke, L., Murugaiyan, J., von Bergen, M., Betzel, C., Saborowski, R. (2008) Autoproteolytic stability of a trypsin   from the marine crab Cancer pagurus. Biochem. Biophys. Res. Commun. 370, 566- 571. Hehemann, J.H., Redecke, L., Perbandt, M., Saborowski, R., Betzel, C. (2007) Crystalliza- tion and preliminary X-ray diffraction studies of trypsin-like proteinases from the gastric fluid of the marine crab Cancer pagurus. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. 1, 242–245 Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J., Steigemann, W. (1974) Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor II. Crystallographic refinement at 1.9 A resolution. J. Mol. Biol. 89, 73–101. Jungbauer, A., Kaar, W. (2007) Current status of technical protein refolding. J. Biotech. 128, 587-596. Kim, H.R., Meyers, S.P., Godber, J.S. (1992) Purification and characterization of anionic trypsins from the hepatopancreas of crayfish. Procambarus clarkii. Comp. Biochem. Physiol. 103B (2): 391-398. King, L.A., Possee, R.D. (1992) The baculovirus expression system: a laboratory guide. (Chapman y Hall eds.), Springer, 229 pp. Kirpichnikov, V.S., Muske, G.A. (1980) The adapta- tive value of biochemical polymorphism in animal and plant populations. Genética 52/53, 183-193. Klein, B., Le Moullac, G., Sellos, D., Van Wormhoudt, A. (1996) Molecular cloning and sequencing of trypsin cDNA from Penaeus vannamei (Crustacea, Decapoda): use in assessing gene expression during the moult cycle. Int. J. Biochem. Cell Biol. 28, 551–563. Klein, B., Sellos, D., Van-Wormhoudt, A. (1998) Genomic organization and polymorphism of a Crustacean trypsin multi-gene family. Gene, 216, 123-129. Klomklao, S., Benjakul, S., Visessanguan, W., Kishimura, H., Simpson, B.K. (2007) Trypsin from the pyloric caeca of bluefish (Pomatomus saltatrix). Comp. Biochem. Physiol. 148B, 382-389. Klomklao, S., Benjakul, S., Visessanguan, W., Kishimura, H., Simpson, B.K., Saeki, H. (2006) Trypsin from yellowfin tuna (Thunnus albacores) spleen: purification and characterization. Comp. Biochem. Physiol. 144B, 47-56. Klomklao, S., Kishimura, H., Nonami, Y., Benjakul, S. (2009) Biochemical properties of two isoforms of trypsin purified from the intestine of skipjack tuna (Katsuwonus pelamis). Food Chemistry 115, 155-162. Kossiakoff, A.A., Chambers, J.L., Kay, L.M., Stroud, R.M. (1977) Structure of bovine trypsinoge at 1.9 Å resolutions. Biochemistry 16, 654-664. Lam, W., Coast, G.M., Rayne, R.C. (2000) Characte- risation of multiple tripsins from the midgut of Locusta migratoria. Insect Biochem. Mol. Biol. 30, 85–94. LaVoie, M.J., Ostaszewski, B.L., Weihofen, A., Schlossmacher, M.G., Selkoe, D.J. (2005) Dopamine covalently modifies and functionally inactivates parkin. Nat. Med. 11(11): 1214-21. Lu, B., Zhou, L., Cai, Q., Hara, K., Maeda, A., Su, W., Cao, M. (2008) Purification and charac- terization of trypsins from the pyloric caeca of mandarin fish (Siniperca chuatsi). Food chemistry 110, 352-360. Martínez, A., Olsen, R.L., Serra, J.L. (1988) Purification and characterization of two trypsin-like enzymes from the digestive tract of anchovy Engraulis encrasicholus. Comp. Biochem. Physiol. 91B (4): 677-684. Muhlia-Almazán, A., Sánchez-Paz, A., García- Carreño, F.L. (2008) Invertebrate trypsins: a review. J. Comp. Physiol. 178B, 655–672. Northrup, J.H., Kunitz, M. (1931) Isolation of protein crystals possessing tryptic activity. Science 73, 262–263. Northrup, J.H., Kunitz, M., Herriott, R.M. (1948) Crystalline enzymes. Columbia University Press, New York. Ohlsson, K., Tegner, H. (1973) Anionic and cationic dog trypsin: Isolation and partial character- rization. Biochim. Biophys. Acta 317(2): 328- 337. Patthy, L. (1999) Genome evolution and the evolution of exon shuffling: a review. Gene 238, 103-114. Perdomo-Morales, R., Montero-Alejo, V., Perera, E., Pardo-Ruiz, Z., Alonso-Jiménez, E. (2007) Phenoloxidase activity in the hemolymph of the spiny lobster Panulirus argus. Fish Shell Immunol. 23, 1187-1195. Perdomo-Morales, R., Montero-Alejo, V., Perera, E, Pardo-Ruiz, Z., Alonso-Jiménez, E. (2008) Hemocyanin-derived phenoloxidase activity in the hemolymph of the spiny lobster Panulirus argus. Biochim. Biophys. Acta 1780, 652-658. Perera, E., Moyano, F.J., Díaz, M, Perdomo- Morales, R., Montero-Alejo, V., Alonso- Jiménez, E, Carrillo, O., Galich, G. (2008) Polymorphism and partial characterization of digestive enzymes in the spiny lobster Panulirus argus. Comp. Biochem. Physiol. 150B, 247-254. Perera, E., Moyano, F.J., Rodríguez-Viera, L., Cer- vantes, A, Martínez-Rodríguez, G., Mancera, J.M. (2010) In vitro digestion of protein sources by crude enzyme extracts of the spiny lobster Panulirus argus (Latreille, 1804) hepatopancreas with different trypsin isoen- zyme patterns. Aquaculture 310, 178-185. Perera, E., Pons, T., Hernández, D., Moyano, F.J., Martínez-Rodríguez, G., Mancera, J.M. (2010) New members of the brachyurins Purificación de isoformas de proteasas tipo tripsina de crustáceos            Rodríguez‐Casariego, Perdomo‐Morales, Perera(2012)   8  family in lobster include a trypsin-like enzyme with amino acid substitutions in the substrate-binding pocket. FEBS J. 277, 3489-3501. Perona, J.J., Craik, C.S. (1995) Structural basis of substrate specificity in the serine proteases. Protein Sci. 4, 337–360. Perona, J.J., Tsu, C.A., Craik, C.S., Fletterick, R.J. (1997) Crystal structure of an ecotin- collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry 36, 5381-5392. Polanowski, A., Wilimowska-Pelc, A., Kowalska, J., Grybel, J., Zelazko, M., Wilusz, T. (2003) Non-conventional affinity chromatography of serine proteinases and their inhibitors. Acta Biochem. Pol. 50(3): 765-773 Puigserver, A., Desnuelle, P. (1971) Identification of an anionic trypsinogen in bovine pancreas. Biochim. Biophys. Acta 236(2): 499-502. Rescigno, A., Sollai, F., Pisu, B., Rinaldi, A., Sanjust, E. (2002) Tyrosinase inhibition: general and applied aspects. J. Enzyme Inhib. Med. Chem. 17(4), 207-18. Roy, P., Colas, B., Durand, P. (1996) Purification, kinetical and molecular characterization of a collagenolytic protease from greenshore crab (Carcinus maenas) digestive gland. Comp. Biochem. Physiol. 115B (1): 97-95. Rungruangsak-Torrissen, K., Male, R. (2000) Trypsin isozymes: Development, digestion and structure. En: Seafood Enzymes, utilization and influence on post-harvest seafood quality. (NF Haard, BK Simpson eds.) Marcel Dekker, Inc., New York, 215– 269 pp. Sainz, J.C., Córdova-Murueta, J.H. (2009) Activity of trypsin from Litopenaeus vannamei. Aquaculture 290, 190-195. Sainz, J.C., García-Carreño, F.L., Córdova- Murueta, J.H., Cruz-Hernández, P. (2005) Penaeus vannamei (Boone, 1931) isotrypsins, genotype and modulation. J. Exp. Mar. Biol. Ecol. 326, 105–113. Sainz, J.C., García-Carreño, F.L., Hernández-Cortés, P. (2004) Penaeus vannamei isotrypsins: purification and characterization. Comp. Biochem. Physiol. 138B, 155–162. Schwarzenberger, A., Zitt, A., Kroth, P., Mueller, S., Von Elert, E. (2010) Gene expression and activity of digestive proteases in Daphnia: effects of cyanobacterial protease inhibitors. BMC Physiology 10, 6. Scopes, R.K. (1994) Protein purification, principles and practice. 3rd ed., Springer Advanced Text in Chemistry, New York, USA, 439 pp. Sjödahl, J., Emmer, A., Vincent, J, Roeraadea, J. (2002) Characterization of proteinases from Antarctic krill (Euphausia superba). Protein Expres. Purif. 26, 153-161. Sorensen, P.H., Mortensen, K.K. (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnology 115, 113-128. Sweet, R.M., Wright, H.T., Janin, J., Chothia, C.H., Blow, D.M. (1974) Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-Å resolution. Biochemistry 13, 4212-4228. Tsai, I., Liu, K.C., Chuang, J. (1991) The midgut chymotrypsins of shrimps (Penaeusmonodon, Penaeusjaponicus and Penaeuspenicillatus). Biochim. Biophys. Acta 1080, 59–67. Tsu, C.A., Craik, C.S. (1998) Brachyurins. En: Handbook of Proteolytic Enzymes. (AJ Barrett, ND Rawlings, JF Woessner, eds.) Academic Press, San Diego, CA, USA, 25-30 pp. Tsu, C.A., Perona, J.J., Fletterick, R.J., Craik, C.S. (1997) Structural basis for the broad substrate specificity of fiddler crab collagenolytic serine protease. Biochemistry 36, 5393-5401. Voytek, P., Gjessing, E.C. (1971) Studies of an anionic trypsinogen and its active enzyme from porcine pancreas. J Biol. Chem. 246(2): 508-516. Walsh, K.A., Kauffman, D.L., Sampath-Kumar, K.S.V., Neurath, H. (1964) On the structure and function of bovine trypsinogen and trypsin. Proc. Natl. Acad. Sci. USA 51, 301– 308. Walsh, K.A., Wilcox, P.E. (1970) Serine proteinases. Meth. Enzymol. 19, 31–41. Whitehead, R.E., Ferrer, J.V., Javitch, J.A, Justice, J.B. (2001) Reaction of oxidized dopamine with endogenous cysteine residues in the human dopamine transporter. J. Neurochem. 76, 1242-1251. Wu, Z., Jiang, G., Xiang, P., Xu, H. (2008) Anionic trypsin from North Pacific krill (Euphausia pacifica): purification and characterization. Int. J. Pept. Res. Ther. 14, 113-120. Yoshida, K., Shinmyo, A. (2000) Transgene expression systems in plant, a natural bioreactor. Journal of Bioscience and Bioengineering 90, 353-362. Zwiling, R.G., Pfleiderer, H., Sonneborn, H., Kraft, V., Stucky, I. (1969) The evolution of endopeptidases: Common and different traits of bovine and crayfish trypsin. Comp. Biochem. Physiol. 28, 1275-1287.
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