메뉴 건너뛰기




Volumn 128, Issue 4, 2011, Pages 847-853

A novel aspartic protease from the viscera of Sardinelle (Sardinella aurita): Purification and characterisation

Author keywords

Aspartic protease; Biochemical characterisation; Purification; Sardinelle (Sardinella aurita); Viscera

Indexed keywords

ACIDIC PROTEASE; AMINO ACID SEQUENCE; ASPARTIC PEPTIDASE; ASPARTIC PROTEASE; CHARACTERISATION; HAEMOGLOBINS; N-TERMINALS; OPTIMUM PH; PH STABILITY; PHENYLMETHYLSULFONYL FLUORIDE; PROTEASE ACTIVITIES; PURIFIED ENZYME; ROOM TEMPERATURE; SARDINELLA; SDS-PAGE; SINGLE BAND; SOYBEAN TRYPSIN INHIBITOR; SPECIFIC ACTIVITY; SULPHATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; VISCERA;

EID: 79958027388     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.03.104     Document Type: Article
Times cited : (34)

References (45)
  • 2
    • 70549097053 scopus 로고    scopus 로고
    • Characterisation of full-length sequenced cDNA inserts (FLIcs) from Atlantic salmon (Salmo salar)
    • Andreassen, R., Lunner, S., & Hoyheim, B. (2009). Characterisation of full-length sequenced cDNA inserts (FLIcs) from Atlantic salmon (Salmo salar). BMC Genomics, 10, 502.
    • (2009) BMC Genomics , vol.10 , pp. 502
    • Andreassen, R.1    Lunner, S.2    Hoyheim, B.3
  • 3
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain, and the cathepsin with hemoglobin
    • Anson, M. L. (1938). The estimation of pepsin, trypsin, papain, and the cathepsin with hemoglobin. The Journal of General Physiology, 22, 79-89.
    • (1938) The Journal of General Physiology , vol.22 , pp. 79-89
    • Anson, M.L.1
  • 5
    • 79952574045 scopus 로고    scopus 로고
    • Purification and characterisation of three trypsin isoforms from viscera of sardinelle (Sardinella aurita)
    • doi:10.1007/s10695-010-9424-5
    • Ben Khaled, H., Jellouli, K., Souissi, N., Ghorbel, S., Barkia, A., & Nasri, M. (2010). Purification and characterisation of three trypsin isoforms from viscera of sardinelle (Sardinella aurita). Fish Physiology and Biochemistry, doi:10.1007/s10695-010-9424-5.
    • (2010) Fish Physiology and Biochemistry
    • Ben Khaled, H.1    Jellouli, K.2    Souissi, N.3    Ghorbel, S.4    Barkia, A.5    Nasri, M.6
  • 6
    • 77956616007 scopus 로고    scopus 로고
    • Low molecular weight serine protease from the viscera of sardinelle (Sardinella aurita) with collagenolytic activity: Purification and characterisation
    • Ben Khaled, H., Nasri, R., Bougatef, A., Ghorbel, S., & Nasri, M. (2011). Low molecular weight serine protease from the viscera of sardinelle (Sardinella aurita) with collagenolytic activity: Purification and characterisation. Food Chemistry, 124, 788-794.
    • (2011) Food Chemistry , vol.124 , pp. 788-794
    • Ben Khaled, H.1    Nasri, R.2    Bougatef, A.3    Ghorbel, S.4    Nasri, M.5
  • 7
    • 0025134312 scopus 로고
    • Cloning, sequence and expression of rat cathepsin D
    • Birch, N. P., & Loh, Y. P. (1990). Cloning, sequence and expression of rat cathepsin D. Nucleic Acids Research, 18, 6445-6446. (Pubitemid 20379220)
    • (1990) Nucleic Acids Research , vol.18 , Issue.21 , pp. 6445-6446
    • Birch, N.P.1    Loh, Y.P.2
  • 8
    • 36148982627 scopus 로고    scopus 로고
    • Pepsinogen and pepsin from the stomach of smooth hound (Mustelus mustelus): Purification, characterization and amino acid terminal sequences
    • DOI 10.1016/j.foodchem.2007.08.077, PII S0308814607009053
    • Bougatef, A., Balti, R., Ben Zaied, S., Souissi, N., & Nasri, M. (2008). Pepsinogen and pepsin from the stomach of smooth hound (Mustelus mustelus): Purification, characterisation and amino acid terminal sequences. Food Chemistry, 107, 777-784. (Pubitemid 350116382)
    • (2008) Food Chemistry , vol.107 , Issue.2 , pp. 777-784
    • Bougatef, A.1    Balti, R.2    Zaied, S.B.3    Souissi, N.4    Nasri, M.5
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, 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.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 10
    • 0029129455 scopus 로고
    • Aspartic proteinases (cyprosins) from Cynara cardunculus spp. Flavescens cv. cardoon; purification, characterisation, and tissue-specific expression
    • Brodelius, P. E., Cordeiro, M. C., & Pais, M. S. (1995). Aspartic proteinases (cyprosins) from Cynara cardunculus spp. Flavescens cv. cardoon; purification, characterisation, and tissue-specific expression. Advances in Experimental Medicine and Biology, 362, 255-266.
    • (1995) Advances in Experimental Medicine and Biology , vol.362 , pp. 255-266
    • Brodelius, P.E.1    Cordeiro, M.C.2    Pais, M.S.3
  • 11
    • 0030814882 scopus 로고    scopus 로고
    • Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss
    • Brooks, S., Tyler, C. R., Carnevali, O., Coward, K., & Sumpter, J. P. (1997). Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss. Gene, 201, 45-54.
    • (1997) Gene , vol.201 , pp. 45-54
    • Brooks, S.1    Tyler, C.R.2    Carnevali, O.3    Coward, K.4    Sumpter, J.P.5
  • 12
    • 0346058040 scopus 로고    scopus 로고
    • Characterization of acidic proteolytic enzymes from Monterey sardine (Sardinops sagax caerulea) viscera
    • DOI 10.1016/j.foodchem.2003.07.008
    • Castillo-Yanez, F. J., Pacheco-Aguilar, R., Garcia-Carreno, F. L., & Toro, M. A. N. D. (2004). Characterisation of acidic proteolytic enzymes from Monterey sardine (Sardinops sagax caerulea) viscera. Food Chemistry, 85, 343-350. (Pubitemid 38067249)
    • (2004) Food Chemistry , vol.85 , Issue.3 , pp. 343-350
    • Castillo-Yanez, F.J.1    Pacheco-Aguilar, R.2    Garcia-Carreno, F.L.3    Navarrete-Del, T.M.D.L.A.4
  • 13
    • 0032924303 scopus 로고    scopus 로고
    • Isolation, characterization and molecular cloning of cathepsin D from lizard ovary: Changes in enzyme activity and mRNA expression throughout ovarian cycle
    • DOI 10.1002/(SICI)1098-2795(199902)52:2<126::AID-MRD2>3.0.CO;2-O
    • De Stasio, R., Borrelli, L., Kille, P., Parisi, E., & Filosa, S. (1999). Isolation, characterisation and molecular cloning of cathepsin D from lisard ovary: Changes in enzyme activity and mRNA expression throughout ovarian cycle. Molecular Reproduction and Development, 52, 126-134. (Pubitemid 29013380)
    • (1999) Molecular Reproduction and Development , vol.52 , Issue.2 , pp. 126-134
    • De Stasio, R.1    Borrelli, L.2    Kille, P.3    Parisi, E.4    Filosa, S.5
  • 14
    • 1042266273 scopus 로고    scopus 로고
    • Purification and characterisation of an acidic protease from the viscera of bolti fish (Tilapia nilotica)
    • El-Beltagy, A. E., El-Adawy, T. A., Rahma, E. H., & El-Bedawey, A. A. (2004). Purification and characterisation of an acidic protease from the viscera of bolti fish (Tilapia nilotica). Food Chemistry, 86, 33-39.
    • (2004) Food Chemistry , vol.86 , pp. 33-39
    • El-Beltagy, A.E.1    El-Adawy, T.A.2    Rahma, E.H.3    El-Bedawey, A.A.4
  • 16
    • 37349061026 scopus 로고    scopus 로고
    • Characterization and expression of the pepsinogen C gene and determination of pepsin-like enzyme activity from orange-spotted grouper (Epinephelus coioides)
    • DOI 10.1016/j.cbpb.2007.09.017, PII S1096495907003806
    • Feng, S., Li, W., & Lin, H. (2008). Characterisation and expression of the pepsinogen C gene and determination of pepsin-like enzyme activity from orange-spotted grouper (Epinephelus coioides). Comparative Biochemistry and Physiology, 149B, 275-284. (Pubitemid 350300009)
    • (2008) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology , vol.149 , Issue.2 , pp. 275-284
    • Feng, S.1    Li, W.2    Lin, H.3
  • 18
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors
    • DOI 10.1006/abio.1993.1457
    • Garcia-Carreno, F. L., Dimes, L. E., & Haard, N. F. (1993). Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinases inhibitors. Analytical Biochemistry, 214, 65-69. (Pubitemid 23300354)
    • (1993) Analytical Biochemistry , vol.214 , Issue.1 , pp. 65-69
    • Garcia-Carreno, F.L.1    Dimes, L.E.2    Haard, N.F.3
  • 20
    • 0030749449 scopus 로고    scopus 로고
    • Bacterial aspartic proteinases
    • DOI 10.1016/S0014-5793(97)00547-4, PII S0014579397005474
    • Hill, J., & Phylip, L. H. (1997). Bacterial aspartic proteinases. FEBS Letters, 409, 357-360. (Pubitemid 27285885)
    • (1997) FEBS Letters , vol.409 , Issue.3 , pp. 357-360
    • Hill, J.1    Phylip, L.H.2
  • 22
    • 64549088906 scopus 로고    scopus 로고
    • Molecular cloning, characterisation and expression analysis of cathepsin D gene from turbot Scophthalmus maximus
    • Jia, A., & Zhang, X. H. (2009). Molecular cloning, characterisation and expression analysis of cathepsin D gene from turbot Scophthalmus maximus. Fish Shellfish Immunology, 26, 606-613.
    • (2009) Fish Shellfish Immunology , vol.26 , pp. 606-613
    • Jia, A.1    Zhang, X.H.2
  • 23
    • 0030821517 scopus 로고    scopus 로고
    • Preliminary characterisation of an Onchocerca volvulus aspartic protease
    • DOI 10.1016/S0020-7519(97)00069-6, PII S0020751997000696
    • Jolodar, A., & Miller, D. J. (1997). Preliminary characterisation of an Onchocerca volvulus aspartic protease. International Journal for Parasitology, 27, 1087-1090. (Pubitemid 27423697)
    • (1997) International Journal for Parasitology , vol.27 , Issue.9 , pp. 1087-1090
    • Jolodar, A.1    Miller, D.J.2
  • 24
    • 0024586972 scopus 로고
    • Difference of activation processes and structure of activation peptides in human pepsinogens A and progastricsin
    • Kageyama, T., Ichinose, M., Miki, K., Athauda, S. B., Tanji, M., & Takahashi, K. (1989). Difference of activation processes and structure of activation peptides in human pepsinogens A and progastricsin. Journal of Biochemistry, 105, 15-22. (Pubitemid 19036162)
    • (1989) Journal of Biochemistry , vol.105 , Issue.1 , pp. 15-22
    • Kageyama, T.1    Ichinose, M.2    Miki, K.3    Athauda, S.B.4    Tanji, M.5    Takahashi, K.6
  • 28
    • 1842422074 scopus 로고    scopus 로고
    • Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus)
    • Komai, T., Kawabata, C., Amano, M., Lee, B. R., & Ichishima, E. (2004). Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus). Comparative Biochemistry and Physiology, 137, 373-382.
    • (2004) Comparative Biochemistry and Physiology , vol.137 , pp. 373-382
    • Komai, T.1    Kawabata, C.2    Amano, M.3    Lee, B.R.4    Ichishima, E.5
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 36749023464 scopus 로고    scopus 로고
    • An acidic protease from the grass carp intestine (Ctenopharyngodon idellus)
    • Liu, Z.-y., Wang, Z., & Zhang, J. (2008). An acidic protease from the grass carp intestine (Ctenopharyngodon idellus). Comparative Biochemistry and Physiology, 149B, 83-90.
    • (2008) Comparative Biochemistry and Physiology , vol.149 B , pp. 83-90
    • Liu, Z.-Y.1    Wang, Z.2    Zhang, J.3
  • 34
    • 0034778987 scopus 로고    scopus 로고
    • Follow the protons: A low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases
    • Northrop, D. B. (2001). Follow the protons: A low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases. Accounts of Chemical Research, 34, 790-797.
    • (2001) Accounts of Chemical Research , vol.34 , pp. 790-797
    • Northrop, D.B.1
  • 35
    • 0031516896 scopus 로고    scopus 로고
    • Properties of pepsin and trypsin isolated from the digestive tract of Parona signata palometa
    • Pavlisko, A., Rial, A., Vecchi, D. E. S., & Coppes, Z. (1997). Properties of pepsin and trypsin isolated from the digestive tract of Parona signata palometa. The Journal of Food Biochemistry, 21, 289-308.
    • (1997) The Journal of Food Biochemistry , vol.21 , pp. 289-308
    • Pavlisko, A.1    Rial, A.2    Vecchi, D.E.S.3    Coppes, Z.4
  • 36
    • 0026437443 scopus 로고
    • Molecular cloning and functional characterisation of chicken cathepsin D, a key enzyme for yolk formation
    • Retzek, H., Steyrer, E., Sanders, E. J., Nimpf, J., & Schneider, W. J. (1992). Molecular cloning and functional characterisation of chicken cathepsin D, a key enzyme for yolk formation. DNA and Cell Biology, 11, 661-672.
    • (1992) DNA and Cell Biology , vol.11 , pp. 661-672
    • Retzek, H.1    Steyrer, E.2    Sanders, E.J.3    Nimpf, J.4    Schneider, W.J.5
  • 37
    • 2942512921 scopus 로고    scopus 로고
    • Structure and function of plant aspartic proteinases
    • DOI 10.1111/j.1432-1033.2004.04136.x
    • Simões, I., & Faro, C. (2004). Structure and function of plant aspartic proteinases. European Journal of Biochemistry, 271, 2067-2075. (Pubitemid 38747976)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.11 , pp. 2067-2075
    • Simoes, I.1    Faro, C.2
  • 38
    • 0346128071 scopus 로고    scopus 로고
    • Digestive proteinases from marine animals
    • N. F. Haard & B. K. Simpson (Eds.), New York: Marcel Dekker
    • Simpson, B. K. (2000). Digestive proteinases from marine animals. In N. F. Haard & B. K. Simpson (Eds.), Seafood enzymes: Utilisation and influence on postharvest seafood quality (pp. 531-540). New York: Marcel Dekker.
    • (2000) Seafood Enzymes: Utilisation and Influence on Postharvest Seafood Quality , pp. 531-540
    • Simpson, B.K.1
  • 39
    • 0022494721 scopus 로고
    • Gastric proteases of the Greenland cod (Gadus ogac). II. Structural properties
    • Squires, E. J., Haard, N. F., & Feltham, L. A. W. (1986). Gastric proteases of the Greenland cod (Gadus ogac). II. Structural properties. Biochemistry and Cell Biology, 64, 215-222.
    • (1986) Biochemistry and Cell Biology , vol.64 , pp. 215-222
    • Squires, E.J.1    Haard, N.F.2    Feltham, L.A.W.3
  • 40
    • 33847220031 scopus 로고    scopus 로고
    • Purification and characterisation of pepsinogens from the gastric mucosa of African coelacanth, Latimeria chalumnae, and properties of the major pepsins
    • Tanji, M., Yakabe, E., Kageyama, T., Yokobori, S. I., Ichinose, M., Miki, K., et al. (2007). Purification and characterisation of pepsinogens from the gastric mucosa of African coelacanth, Latimeria chalumnae, and properties of the major pepsins. Comparative Biochemistry and Physiology, 146B, 412-420.
    • (2007) Comparative Biochemistry and Physiology , vol.146 B , pp. 412-420
    • Tanji, M.1    Yakabe, E.2    Kageyama, T.3    Yokobori, S.I.4    Ichinose, M.5    Miki, K.6
  • 41
    • 0029002927 scopus 로고
    • A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp
    • Toogood, H. S., Prescott, M., & Daniel, R. M. (1995). A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp. Biochemical Journal, 307, 783-789.
    • (1995) Biochemical Journal , vol.307 , pp. 783-789
    • Toogood, H.S.1    Prescott, M.2    Daniel, R.M.3
  • 42
    • 3242790919 scopus 로고    scopus 로고
    • Proteinases from gastric mucosa of European Sheatfish (Silirus glanis L.)
    • Ulitina, N. N., & Proskuryakov, M. T. (2004). Proteinases from gastric mucosa of European Sheatfish (Silirus glanis L.). Applied Biochemistry and Microbiology, 40, 30-34.
    • (2004) Applied Biochemistry and Microbiology , vol.40 , pp. 30-34
    • Ulitina, N.N.1    Proskuryakov, M.T.2
  • 43
    • 33748205449 scopus 로고    scopus 로고
    • Purification and characterisation of stomach protease from the turbot (Scophthalmus maximus L.)
    • Wang, H. Y., Wang, Y. J., Wang, Q. Y., Xue, C. H., & Sun, M. (2006). Purification and characterisation of stomach protease from the turbot (Scophthalmus maximus L.). Fish Physiology and Biochemistry, 32, 179-188.
    • (2006) Fish Physiology and Biochemistry , vol.32 , pp. 179-188
    • Wang, H.Y.1    Wang, Y.J.2    Wang, Q.Y.3    Xue, C.H.4    Sun, M.5
  • 44
    • 60749092009 scopus 로고    scopus 로고
    • Identification of pepsinogens and pepsins from the stomach of European eel (Anguilla anguilla)
    • Wu, T., Sun, L. C., Du, C. H., Cai, Q. F., Zhang, Q. B., Su, W. J., et al. (2009). Identification of pepsinogens and pepsins from the stomach of European eel (Anguilla anguilla). Food Chemistry, 115, 137-142.
    • (2009) Food Chemistry , vol.115 , pp. 137-142
    • Wu, T.1    Sun, L.C.2    Du, C.H.3    Cai, Q.F.4    Zhang, Q.B.5    Su, W.J.6
  • 45
    • 33847136084 scopus 로고    scopus 로고
    • Purification and characterization of sea bream (Sparus latus Houttuyn) pepsinogens and pepsins
    • DOI 10.1016/j.foodchem.2006.09.021, PII S0308814606007382
    • Zhou, Q., Fu, X. P., Zhang, L. J., Su, W. J., & Cao, M. J. (2007). Purification and characterisation of sea bream (Sparus latus Houttuyn) pepsinogens and pepsins. Food Chemistry, 103, 795-801. (Pubitemid 46283225)
    • (2007) Food Chemistry , vol.103 , Issue.3 , pp. 795-801
    • Zhou, Q.1    Fu, X.-P.2    Zhang, L.-J.3    Su, W.-J.4    Cao, M.-J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.