메뉴 건너뛰기




Volumn 138, Issue 2, 2004, Pages 155-162

Penaeus vannamei isotrypsins: Purification and characterization

Author keywords

Invertebrate trypsin; Isoenzymes; Penaeus vannamei

Indexed keywords

AMIDE; CALCIUM ION; COMPLEMENTARY DNA; GLYCOPROTEIN; ISOTRYPSIN A; ISOTRYPSIN B; ISOTRYPSIN C; TRYPSIN; UNCLASSIFIED DRUG;

EID: 2942607953     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2004.03.002     Document Type: Article
Times cited : (58)

References (46)
  • 3
    • 0001781085 scopus 로고    scopus 로고
    • In vitro protein digestion, and growth of Atlantic salmon with different trypsin isoenzymes
    • Bassompierre M., Ostenfled T.H., McLean E. In vitro protein digestion, and growth of Atlantic salmon with different trypsin isoenzymes. Aquacult. Int. 6:1998;47-56
    • (1998) Aquacult. Int. , vol.6 , pp. 47-56
    • Bassompierre, M.1    Ostenfled, T.H.2    McLean, E.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principles of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principles of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0346764650 scopus 로고    scopus 로고
    • Purification and characterization of two anionic trypsins from the hepatopancreas of carp
    • Cao M.J., Osatomi K., Suzuki M., Hara K., Tachibana K., Ishihara T. Purification and characterization of two anionic trypsins from the hepatopancreas of carp. Fish. Sci. 66:2000;1172-1179
    • (2000) Fish. Sci. , vol.66 , pp. 1172-1179
    • Cao, M.J.1    Osatomi, K.2    Suzuki, M.3    Hara, K.4    Tachibana, K.5    Ishihara, T.6
  • 8
    • 0242349740 scopus 로고    scopus 로고
    • Digestive enzymes present in crustacean feces as a tool for biochemical, physiological, and ecological studies
    • Córdova-Murueta J., García-Carreño F.L., Navarrete del Toro M.A. Digestive enzymes present in crustacean feces as a tool for biochemical, physiological, and ecological studies. J. Exp. Mar. Biol. Ecol. 297:2003;43-56
    • (2003) J. Exp. Mar. Biol. Ecol. , vol.297 , pp. 43-56
    • Córdova-Murueta, J.1    García-Carreño, F.L.2    Navarrete Del Toro, M.A.3
  • 9
    • 0025264947 scopus 로고
    • Purification and characterization of a trypsin like enzyme from the midgut gland of the Atlantic blue crab, Callinectes sapidus
    • Dendiger J.E., O'Connor K.L. Purification and characterization of a trypsin like enzyme from the midgut gland of the Atlantic blue crab, Callinectes sapidus. Comp. Biochem. Physiol. B. 95:1990;525-530
    • (1990) Comp. Biochem. Physiol. B , vol.95 , pp. 525-530
    • Dendiger, J.E.1    O'Connor, K.L.2
  • 10
    • 0007140787 scopus 로고
    • Trypsin like enzyme from sand crab (Portunus pelagicus): Purification and characterization
    • Dionysius D.A., Hoek K.S., Milne K.S., Slattery S.L. Trypsin like enzyme from sand crab (Portunus pelagicus): purification and characterization. J. Food Sci. 58:1993;780-792
    • (1993) J. Food Sci. , vol.58 , pp. 780-792
    • Dionysius, D.A.1    Hoek, K.S.2    Milne, K.S.3    Slattery, S.L.4
  • 11
    • 0027046986 scopus 로고
    • Live under extreme condition: Aspect of evolutionary adaptation to temperature in crustacean proteases
    • Dittrich B.U. Live under extreme condition: aspect of evolutionary adaptation to temperature in crustacean proteases. Polar Biol. 12:1992;269-274
    • (1992) Polar Biol. , vol.12 , pp. 269-274
    • Dittrich, B.U.1
  • 12
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger B.F., Kokowsky N., Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95:1961;271-278
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 13
    • 0040832668 scopus 로고    scopus 로고
    • Effect of feed diets on digestive proteases from the hepatopancreas of the white shrimp (Penaeus vannamei)
    • Ezquerra J.M., García-Carreño L.F., Haard N. Effect of feed diets on digestive proteases from the hepatopancreas of the white shrimp (Penaeus vannamei). J. Food Biochem. 21:1997;401-419
    • (1997) J. Food Biochem. , vol.21 , pp. 401-419
    • Ezquerra, J.M.1    García-Carreño, L.F.2    Haard, N.3
  • 14
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors
    • García-Carreño F., Dimes N., Haard N. Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors. Anal. Biochem. 214:1993;65-69
    • (1993) Anal. Biochem. , vol.214 , pp. 65-69
    • García-Carreño, F.1    Dimes, N.2    Haard, N.3
  • 15
    • 0019336174 scopus 로고
    • Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator
    • Grant G.A., Henderson K.O., Eisen A.Z., Bradshaw R.A. Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator. Biochemistry. 19:1980;4653-4659
    • (1980) Biochemistry , vol.19 , pp. 4653-4659
    • Grant, G.A.1    Henderson, K.O.2    Eisen, A.Z.3    Bradshaw, R.A.4
  • 16
    • 0032808833 scopus 로고    scopus 로고
    • Purification and partial characterization of the pancreatic proteolytic enzymes trypsin, chymotrypsin and elastase from the chicken
    • Guyonnet V., Thuscik F., Long P.L., Polanowski L.A., Travis J. Purification and partial characterization of the pancreatic proteolytic enzymes trypsin, chymotrypsin and elastase from the chicken. J. Chromatogr. A. 852:1999;217-225
    • (1999) J. Chromatogr. a , vol.852 , pp. 217-225
    • Guyonnet, V.1    Thuscik, F.2    Long, P.L.3    Polanowski, L.A.4    Travis, J.5
  • 18
    • 0029027661 scopus 로고
    • Isolation and characterization of gastric trypsin from the microsomal fraction of porcine gastric antral mucosa
    • Jeohn G.H., Serizawa S., Iwamatsu A., Tahkahashi K. Isolation and characterization of gastric trypsin from the microsomal fraction of porcine gastric antral mucosa. J. Biol. Chem. 270:1995;14748-14755
    • (1995) J. Biol. Chem. , vol.270 , pp. 14748-14755
    • Jeohn, G.H.1    Serizawa, S.2    Iwamatsu, A.3    Tahkahashi, K.4
  • 19
    • 0001633298 scopus 로고
    • Purification and characterization of proteases from digestive tract of grass shrimp (Penaeus monodon)
    • Jiang S.T., Moody M., Chen H.C. Purification and characterization of proteases from digestive tract of grass shrimp (Penaeus monodon). J. Food Sci. 56:1991;322-326
    • (1991) J. Food Sci. , vol.56 , pp. 322-326
    • Jiang, S.T.1    Moody, M.2    Chen, H.C.3
  • 20
    • 0028804028 scopus 로고
    • Isolation and characterization of a trypsin from the slipper lobster, Thenus orientalis (Lund)
    • Johnston D., Hermans J.M., Yellowlees D. Isolation and characterization of a trypsin from the slipper lobster, Thenus orientalis (Lund). Arch. Biochem. Biophys. 324:1995;35-40
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 35-40
    • Johnston, D.1    Hermans, J.M.2    Yellowlees, D.3
  • 21
    • 85007724567 scopus 로고
    • Purification and characterization of serine porteinases from Euphausia superba
    • Kimoto K., Kusuma S., Murakami K. Purification and characterization of serine porteinases from Euphausia superba. Agr. Biol. Chem. 47:1983;2577-2583
    • (1983) Agr. Biol. Chem. , vol.47 , pp. 2577-2583
    • Kimoto, K.1    Kusuma, S.2    Murakami, K.3
  • 22
    • 0029888861 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of trypsin cDNAs from Penaeus vannamei (Crustacea, Decapoda): Use in assessing gene expression during the molt cycle
    • Klein B., Le Moullac G., Sellos D., van Wormhoudt A. Molecular cloning and sequencing of trypsin cDNAs from Penaeus vannamei (Crustacea, Decapoda): use in assessing gene expression during the molt cycle. Int. J. Biochem. Cell. Biol. 28:1996;551-563
    • (1996) Int. J. Biochem. Cell. Biol. , vol.28 , pp. 551-563
    • Klein, B.1    Le Moullac, G.2    Sellos, D.3    Van Wormhoudt, A.4
  • 23
    • 0032541396 scopus 로고    scopus 로고
    • Genomic organization and polymorphism of a crustacean trypsin multi-gene family
    • Klein B., Sellos D., van Wormhoudt A. Genomic organization and polymorphism of a crustacean trypsin multi-gene family. Gene. 216:1998;123-129
    • (1998) Gene , vol.216 , pp. 123-129
    • Klein, B.1    Sellos, D.2    Van Wormhoudt, A.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bactriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bactriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0001740809 scopus 로고
    • A quantitative analysis of digestive enzymes in penaeid shrimp; Influence of diet, age and species
    • Lee P.G., Lawrence A.L. A quantitative analysis of digestive enzymes in penaeid shrimp; influence of diet, age and species. Physiologist. 25:1982;241
    • (1982) Physiologist , vol.25 , pp. 241
    • Lee, P.G.1    Lawrence, A.L.2
  • 26
    • 0037111011 scopus 로고    scopus 로고
    • Ontogenic variations in digestive proteinase activity, RNA and DNA content of larval and postlarval white shrimp Litopenaeus schmitti
    • Lemos D., García-Carreño F., Hernández P., Navarrete del Toro M. Ontogenic variations in digestive proteinase activity, RNA and DNA content of larval and postlarval white shrimp Litopenaeus schmitti. Aquaculture. 214:2002;363-380
    • (2002) Aquaculture , vol.214 , pp. 363-380
    • Lemos, D.1    García-Carreño, F.2    Hernández, P.3    Navarrete Del Toro, M.4
  • 27
    • 0000900599 scopus 로고    scopus 로고
    • Adaptation of trypsin, chymotrypsin and a-amylase to casein level and protein source in Penaeus vannamei (Crustacea Decapoda)
    • Le Moullac G.L., Klein B., Sellos D., van Wormhoudt A. Adaptation of trypsin, chymotrypsin and a-amylase to casein level and protein source in Penaeus vannamei (Crustacea Decapoda). J. Exp. Mar. Biol. Ecol. 208:1996;107-125
    • (1996) J. Exp. Mar. Biol. Ecol. , vol.208 , pp. 107-125
    • Le Moullac, G.L.1    Klein, B.2    Sellos, D.3    Van Wormhoudt, A.4
  • 28
    • 0025131057 scopus 로고
    • The midgut trypsins of shrimp (Penaeus monodon), biology and chemistry
    • Lu P.J., Liu H.C., Tsai I.H. The midgut trypsins of shrimp (Penaeus monodon), biology and chemistry. Hoppe-Seyler. 371:1990;851-857
    • (1990) Hoppe-Seyler , vol.371 , pp. 851-857
    • Lu, P.J.1    Liu, H.C.2    Tsai, I.H.3
  • 30
    • 0024189838 scopus 로고
    • Purification and characterization of two trypsin-like enzymes from the digestive tract of anchovy Engraulis encrasicholus
    • Martínez A., Olsen R.L., Serra J.L. Purification and characterization of two trypsin-like enzymes from the digestive tract of anchovy Engraulis encrasicholus. Comp. Biochem. Physiol. B. 91:1988;677-684
    • (1988) Comp. Biochem. Physiol. B , vol.91 , pp. 677-684
    • Martínez, A.1    Olsen, R.L.2    Serra, J.L.3
  • 31
    • 0027661652 scopus 로고
    • Purification and characterization of a trypsin-like digestive enzyme from spruce budworm (Choristoneura fumfeirana) responsible for the activation of d-endotoxin from Bacillus thuringiensis
    • Milne R., Kaplan H. Purification and characterization of a trypsin-like digestive enzyme from spruce budworm (Choristoneura fumfeirana) responsible for the activation of d-endotoxin from Bacillus thuringiensis. Insect Biochem. Mol. Biol. 23:1993;663-673
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 663-673
    • Milne, R.1    Kaplan, H.2
  • 32
    • 0028815857 scopus 로고
    • Studies on the synthesis and secretion of trypsin in the midgut of Stomoxys calcitrans
    • Moffat M.R., Blakemore D., Lehane M.J. Studies on the synthesis and secretion of trypsin in the midgut of Stomoxys calcitrans. Comp. Biochem. Physiol. B. 110:1995;291-300
    • (1995) Comp. Biochem. Physiol. B , vol.110 , pp. 291-300
    • Moffat, M.R.1    Blakemore, D.2    Lehane, M.J.3
  • 35
    • 0000359399 scopus 로고
    • On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia superba
    • Osnes K., Mohr V. On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia superba. Comp. Biochem. Physiol. B. 82:1985;607-619
    • (1985) Comp. Biochem. Physiol. B , vol.82 , pp. 607-619
    • Osnes, K.1    Mohr, V.2
  • 39
    • 0021707123 scopus 로고
    • Purification and characterization of trypsin from Greenland cod, (Gadus ogac). 1. Kinetic and thermodynamic characterization
    • Simpson B.K., Haard N.F. Purification and characterization of trypsin from Greenland cod, (Gadus ogac). 1. Kinetic and thermodynamic characterization. Can. J. Biochem. Cell. Biol. 62:1984;894-900
    • (1984) Can. J. Biochem. Cell. Biol. , vol.62 , pp. 894-900
    • Simpson, B.K.1    Haard, N.F.2
  • 42
    • 5744235228 scopus 로고
    • Trypsinogen and trypsins of various species
    • Walsh K.A. Trypsinogen and trypsins of various species. Methods Enzymol. 19:1970;41-63
    • (1970) Methods Enzymol. , vol.19 , pp. 41-63
    • Walsh, K.A.1
  • 44
    • 0028282969 scopus 로고
    • Prostatin is a novel serine proteinase from seminal fluid-purification, tissue distribution, and localization in prostate gland
    • Yu J.L., Chao L., Chao J. Prostatin is a novel serine proteinase from seminal fluid-purification, tissue distribution, and localization in prostate gland. J. Biol. Chem. 269:1994;18843-18848
    • (1994) J. Biol. Chem. , vol.269 , pp. 18843-18848
    • Yu, J.L.1    Chao, L.2    Chao, J.3
  • 45
    • 0036185856 scopus 로고    scopus 로고
    • Partial characterization of trypsin-like protease and molecular cloning of a trypsin-like precursor cDNA in salivary glands of Lygus lineolaris
    • Zeng F., Zhu Y., Cohen A. Partial characterization of trypsin-like protease and molecular cloning of a trypsin-like precursor cDNA in salivary glands of Lygus lineolaris. Comp. Biochem. Physiol. B. 131:2002;453-463
    • (2002) Comp. Biochem. Physiol. B , vol.131 , pp. 453-463
    • Zeng, F.1    Zhu, Y.2    Cohen, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.