메뉴 건너뛰기




Volumn 396, Issue 3, 2010, Pages 667-673

Purification, characterization and substrate specificity of a trypsin from the Amazonian fish tambaqui (Colossoma macropomum)

Author keywords

FRET peptide; Processing waste; Specific cleavage site; Tropical fish; Trypsin

Indexed keywords

AMINO ACID DERIVATIVE; ARGININE; DETERGENT; LEUCINE; LYSINE; SERINE; TRYPSIN;

EID: 77953324644     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.04.155     Document Type: Article
Times cited : (36)

References (35)
  • 1
    • 34547894473 scopus 로고    scopus 로고
    • Trypsin
    • A.J. Barrett, N.D. Rawlings, J.F. Woessner Eds, Academic Press, London, second ed
    • S. Norioka, F. Sakiyama, Trypsin. in: A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.), Handbook of Proteolytic Enzymes. Academic Press, London, second ed. 2004, pp. 1483-1488.
    • (2004) Handbook of Proteolytic Enzymes , pp. 1483-1488
    • Norioka, S.1    Sakiyama, F.2
  • 2
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom L. Serine protease mechanism and specificity. Chem. Rev. 102 (2002) 4501-4523
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4523
    • Hedstrom, L.1
  • 3
    • 77956730844 scopus 로고
    • The alimentary canal and digestion in teleosts
    • Kapoor B.G., Smit H., and Verighina I.A. The alimentary canal and digestion in teleosts. Adv. Mar. Biol. 13 (1975) 109-239
    • (1975) Adv. Mar. Biol. , vol.13 , pp. 109-239
    • Kapoor, B.G.1    Smit, H.2    Verighina, I.A.3
  • 7
    • 70350373926 scopus 로고    scopus 로고
    • Surfactants- and oxidants-resistant alkaline proteases from common carp (Cyprinus carpio L.) processing waste
    • Espósito T.S., Amaral I.P.G., Marcuschi M., Carvalho Jr. L.B., and Bezerra R.S. Surfactants- and oxidants-resistant alkaline proteases from common carp (Cyprinus carpio L.) processing waste. J. Food Biochem. 33 (2009) 821-834
    • (2009) J. Food Biochem. , vol.33 , pp. 821-834
    • Espósito, T.S.1    Amaral, I.P.G.2    Marcuschi, M.3    Carvalho Jr., L.B.4    Bezerra, R.S.5
  • 8
    • 33750626823 scopus 로고    scopus 로고
    • Digestive enzyme responses of tambaqui (Colossoma macropomum) fed on different levels of protein and lipid
    • Lundstedt L.C.Almeida.L.M., and Moraes G. Digestive enzyme responses of tambaqui (Colossoma macropomum) fed on different levels of protein and lipid. Aqua. Nutr. 12 (2006) 443-450
    • (2006) Aqua. Nutr. , vol.12 , pp. 443-450
    • Lundstedt, L.C.1    Almeida, L.M.2    Moraes, G.3
  • 9
    • 0007166499 scopus 로고    scopus 로고
    • Characterization of stomach and pyloric caeca proteínases of tambaqui (Colossoma macropomum)
    • Bezerra R.S., Santos J.F., Carvalho Jr. L.B., Lino M.A.S., and Vieira V.L.A. Characterization of stomach and pyloric caeca proteínases of tambaqui (Colossoma macropomum). J. Food Biochem. 24 (2000) 189-199
    • (2000) J. Food Biochem. , vol.24 , pp. 189-199
    • Bezerra, R.S.1    Santos, J.F.2    Carvalho Jr., L.B.3    Lino, M.A.S.4    Vieira, V.L.A.5
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye-binding. Anal. Biochem. 72 (1976) 248
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.1
  • 11
    • 77953324139 scopus 로고    scopus 로고
    • R.J. Leatherbarrow, Grafit. Erithacus Software Limited, 2001.
    • R.J. Leatherbarrow, Grafit. Erithacus Software Limited, 2001.
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 67349161774 scopus 로고    scopus 로고
    • Purification and characteristics of trypsins from cold-zone fish, pacific cod (Gadus macrocephalus) and saffron cod (Eleginus gracilis)
    • Fuchise T., Kishimura H., Sekizaki H., Nonami Y., Kanno G., Klomklao S., Benjakul S., and Chun B.S. Purification and characteristics of trypsins from cold-zone fish, pacific cod (Gadus macrocephalus) and saffron cod (Eleginus gracilis). Food Chem. 116 (2009) 611-616
    • (2009) Food Chem. , vol.116 , pp. 611-616
    • Fuchise, T.1    Kishimura, H.2    Sekizaki, H.3    Nonami, Y.4    Kanno, G.5    Klomklao, S.6    Benjakul, S.7    Chun, B.S.8
  • 15
    • 67349154366 scopus 로고    scopus 로고
    • New alkaline trypsin from the intestine of grey triggerfish (Balistes capriscus) with high activity at low temperature: purification and characterization
    • Jellouli K., Bougatef A., Daassi D., Balti R., Barkia A., and Nasri M. New alkaline trypsin from the intestine of grey triggerfish (Balistes capriscus) with high activity at low temperature: purification and characterization. Food Chem. 116 (2009) 644-650
    • (2009) Food Chem. , vol.116 , pp. 644-650
    • Jellouli, K.1    Bougatef, A.2    Daassi, D.3    Balti, R.4    Barkia, A.5    Nasri, M.6
  • 16
    • 33746508515 scopus 로고    scopus 로고
    • Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): isolation and characterization
    • Kishimura H., Tokuda Y., Yabe M., Klomklao S., Benjakul S., and Ando S. Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): isolation and characterization. Food Chem. 100 (2007) 1490-1495
    • (2007) Food Chem. , vol.100 , pp. 1490-1495
    • Kishimura, H.1    Tokuda, Y.2    Yabe, M.3    Klomklao, S.4    Benjakul, S.5    Ando, S.6
  • 17
    • 34548265208 scopus 로고    scopus 로고
    • Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma)
    • Kishimura H., Klomklao S., Benjakul S., and Chun B.S. Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma). Food Chem. 106 (2008) 194-199
    • (2008) Food Chem. , vol.106 , pp. 194-199
    • Kishimura, H.1    Klomklao, S.2    Benjakul, S.3    Chun, B.S.4
  • 18
    • 33751528620 scopus 로고    scopus 로고
    • Purification and characterization of trypsin from the viscera of sardine (Sardina pilchardus)
    • Bougatef A., Souissi N., Fakhfakh N., Ellouz-Triki Y., and Nasri M. Purification and characterization of trypsin from the viscera of sardine (Sardina pilchardus). Food Chem. 102 (2007) 343-350
    • (2007) Food Chem. , vol.102 , pp. 343-350
    • Bougatef, A.1    Souissi, N.2    Fakhfakh, N.3    Ellouz-Triki, Y.4    Nasri, M.5
  • 19
    • 41949139655 scopus 로고    scopus 로고
    • Purification and characterization of trypsins from the pyloric caeca of mandarin fish (Siniperca chuatsi)
    • Lu B.J., Zhou L.G., Cai Q.F., Hara K., Maeda A., Su W.J., and Cao M.J. Purification and characterization of trypsins from the pyloric caeca of mandarin fish (Siniperca chuatsi). Food Chem. 110 (2008) 352-360
    • (2008) Food Chem. , vol.110 , pp. 352-360
    • Lu, B.J.1    Zhou, L.G.2    Cai, Q.F.3    Hara, K.4    Maeda, A.5    Su, W.J.6    Cao, M.J.7
  • 20
    • 60749087304 scopus 로고    scopus 로고
    • Biochemical properties of two isoforms of trypsin purified from the intestine of skipjack tuna (Katsuwonus pelamis)
    • Klomklao S., Kishimura H., Nonami Y., and Benjakul S. Biochemical properties of two isoforms of trypsin purified from the intestine of skipjack tuna (Katsuwonus pelamis). Food Chem. 115 (2009) 155-162
    • (2009) Food Chem. , vol.115 , pp. 155-162
    • Klomklao, S.1    Kishimura, H.2    Nonami, Y.3    Benjakul, S.4
  • 24
    • 33746738184 scopus 로고    scopus 로고
    • Purification and characterization of trypsins from the spleen of skipjack tuna (Katsuwonus pelamis)
    • Klomklao S., Benjakul S., and Visessanguan W. Purification and characterization of trypsins from the spleen of skipjack tuna (Katsuwonus pelamis). Food Chem. 100 (2007) 1580-1589
    • (2007) Food Chem. , vol.100 , pp. 1580-1589
    • Klomklao, S.1    Benjakul, S.2    Visessanguan, W.3
  • 25
    • 28844501954 scopus 로고    scopus 로고
    • Characteristics of trypsins from the viscera of true sardine (Sardinops melanostictus) and the pyloric ceca of arabesque greenling (Pleuroprammus azonus)
    • Kishimura H., Hayashi K., Miyashita Y., and Nonami Y. Characteristics of trypsins from the viscera of true sardine (Sardinops melanostictus) and the pyloric ceca of arabesque greenling (Pleuroprammus azonus). Food Chem. 97 (2006) 65-70
    • (2006) Food Chem. , vol.97 , pp. 65-70
    • Kishimura, H.1    Hayashi, K.2    Miyashita, Y.3    Nonami, Y.4
  • 26
    • 0031453045 scopus 로고    scopus 로고
    • The molecular evolution of the vertebrate trypsinogens
    • Roach J.C., Wang K., Gan L., and Hood L. The molecular evolution of the vertebrate trypsinogens. J. Mol. Evol. 45 (1997) 640-652
    • (1997) J. Mol. Evol. , vol.45 , pp. 640-652
    • Roach, J.C.1    Wang, K.2    Gan, L.3    Hood, L.4
  • 27
    • 0025009050 scopus 로고
    • Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen structural identity within the trypsin family
    • Huerou I., Wicker C., Guilloteau P., Toullec R., and Puigserver A. Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen structural identity within the trypsin family. Eur. J. Biochem. 193 (1990) 767-773
    • (1990) Eur. J. Biochem. , vol.193 , pp. 767-773
    • Huerou, I.1    Wicker, C.2    Guilloteau, P.3    Toullec, R.4    Puigserver, A.5
  • 28
    • 70349303457 scopus 로고    scopus 로고
    • The use of fluorescence resonance energy transfer (FRET) peptides for measurement of clinically important proteolytic enzymes
    • Carmona A.K., Juliano M.A., and Juliano L. The use of fluorescence resonance energy transfer (FRET) peptides for measurement of clinically important proteolytic enzymes. An. Acad. Bras. Ciênc. 81 3 (2009) 381-392
    • (2009) An. Acad. Bras. Ciênc. , vol.81 , Issue.3 , pp. 381-392
    • Carmona, A.K.1    Juliano, M.A.2    Juliano, L.3
  • 32
    • 72049125244 scopus 로고
    • Mechanisms of action of trypsin and chymotrypsin
    • Kasserra H.P., and Laidler K.J. Mechanisms of action of trypsin and chymotrypsin. Can. J. Chem. 47 (1969) 4031-4039
    • (1969) Can. J. Chem. , vol.47 , pp. 4031-4039
    • Kasserra, H.P.1    Laidler, K.J.2
  • 33
    • 33644902351 scopus 로고    scopus 로고
    • Isolation and characterization of a trypsin fraction from the pyloric ceca of chinook salmon (Oncorhynchus tshawytscha)
    • Kurtovic I., Marshall S.N., and Simpson B.K. Isolation and characterization of a trypsin fraction from the pyloric ceca of chinook salmon (Oncorhynchus tshawytscha). Comp. Biochem. Physiol. B 143 (2006) 432-440
    • (2006) Comp. Biochem. Physiol. B , vol.143 , pp. 432-440
    • Kurtovic, I.1    Marshall, S.N.2    Simpson, B.K.3
  • 34
    • 21244469127 scopus 로고    scopus 로고
    • Atlantic cod trypsins: from basic research to practical applications
    • Gudmundsdóttir A., and Pálsdóttir H.M. Atlantic cod trypsins: from basic research to practical applications. Mar. Biotechnol. 7 (2005) 77-88
    • (2005) Mar. Biotechnol. , vol.7 , pp. 77-88
    • Gudmundsdóttir, A.1    Pálsdóttir, H.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.