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Volumn 12, Issue 6, 2010, Pages 696-707

Aspartic Cathepsin D Endopeptidase Contributes to Extracellular Digestion in Clawed Lobsters Homarus americanus and Homarus gammarus

Author keywords

Aspartic protease; Cathepsin D; Clawed lobster; Protein digestion; Starvation

Indexed keywords

ASPARTIC PROTEASE; CATHEPSIN D; CLAWED LOBSTER; PROTEIN DIGESTION; STARVATION;

EID: 78649654930     PISSN: 14362228     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10126-010-9257-3     Document Type: Article
Times cited : (39)

References (77)
  • 1
    • 33845345472 scopus 로고
    • R-cells and the digestive cycle in Penaeus semisulcatus (Crustacea: Decapoda)
    • Al-Mohanna SY, Nott JA (1987) R-cells and the digestive cycle in Penaeus semisulcatus (Crustacea: Decapoda). Mar Biol 95: 129-137.
    • (1987) Mar Biol , vol.95 , pp. 129-137
    • Al-Mohanna, S.Y.1    Nott, J.A.2
  • 3
    • 0037378157 scopus 로고    scopus 로고
    • Molecular cloning and characterization of cathepsin B from the hepatopancreas of northern shrimp Pandalus borealis
    • Aoki H, Nazmul Ahsan M, Shugo W (2003) Molecular cloning and characterization of cathepsin B from the hepatopancreas of northern shrimp Pandalus borealis. Comp Biochem Physiol B Biochem Mol Biol 134: 681-694.
    • (2003) Comp Biochem Physiol B Biochem Mol Biol , vol.134 , pp. 681-694
    • Aoki, H.1    Nazmul Ahsan, M.2    Shugo, W.3
  • 4
    • 0442298684 scopus 로고    scopus 로고
    • Molecular and enzymatic properties of a cathepsin L-like proteinase with distinct substrate specificity from northern shrimp (Pandalus borealis)
    • Aoki H, Ahsan M, Watabe S (2004) Molecular and enzymatic properties of a cathepsin L-like proteinase with distinct substrate specificity from northern shrimp (Pandalus borealis). J Comp Physiol B-Biochem Syst Environ Physiol 174: 59-69.
    • (2004) J Comp Physiol B-Biochem Syst Environ Physiol , vol.174 , pp. 59-69
    • Aoki, H.1    Ahsan, M.2    Watabe, S.3
  • 5
    • 0001235835 scopus 로고
    • Observations on the feeding mechanism, structure of the gut, and digestive physiology of the European lobster Homarus gammarus
    • Baker PL, Gibson R (1977) Observations on the feeding mechanism, structure of the gut, and digestive physiology of the European lobster Homarus gammarus. J Exp Mar Biol Ecol 26: 297-324.
    • (1977) J Exp Mar Biol Ecol , vol.26 , pp. 297-324
    • Baker, P.L.1    Gibson, R.2
  • 6
    • 0018661114 scopus 로고
    • Cathepsin D: the lysosomal aspartic proteinase
    • Barrett AJ (1979) Cathepsin D: the lysosomal aspartic proteinase. Ciba Found Symp 79: 37-50.
    • (1979) Ciba Found Symp , vol.79 , pp. 37-50
    • Barrett, A.J.1
  • 7
    • 9444261706 scopus 로고    scopus 로고
    • Cathepsin D: the lysosomal aspartic proteinase
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner (Eds.), San Diego: Academic
    • Barrett AJ (1998) Cathepsin D: the lysosomal aspartic proteinase. In: Barrett AJ, Rawlings ND, Woessner JF (eds) Handbook of proteolytic enzymes. Academic, San Diego, pp 37-50.
    • (1998) Handbook of Proteolytic Enzymes , pp. 37-50
    • Barrett, A.J.1
  • 8
    • 0004582738 scopus 로고    scopus 로고
    • Proteolytic enzymes
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner (Eds.), San Diego: Academic
    • Barrett AJ, Rawlings ND, Woessner JF (1998) Proteolytic enzymes. In: Barrett AJ, Rawlings ND, Woessner JF (eds) Handbook of proteolytic enzymes. Academic, San Diego, pp 801-805.
    • (1998) Handbook of Proteolytic Enzymes , pp. 801-805
    • Barrett, A.J.1    Rawlings, N.D.2    Woessner, J.F.3
  • 9
    • 0028866913 scopus 로고
    • Cloning and characterization of the Schistosoma japonicum aspartic proteinase involved in hemoglobin degradation
    • Becker MM, Harrop SA, Dalton JP, Kalinna BH, McManus DP, Brindley PJ (1995) Cloning and characterization of the Schistosoma japonicum aspartic proteinase involved in hemoglobin degradation. J Biol Chem 270: 24496-24501.
    • (1995) J Biol Chem , vol.270 , pp. 24496-24501
    • Becker, M.M.1    Harrop, S.A.2    Dalton, J.P.3    Kalinna, B.H.4    McManus, D.P.5    Brindley, P.J.6
  • 10
    • 29144503154 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis
    • Boldbaatar D, Sikasunge CS, Battsetseg B, Xuan X, Fujisaki K (2006) Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis. Insect Biochem Mol Biol 36: 25-36.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 25-36
    • Boldbaatar, D.1    Sikasunge, C.S.2    Battsetseg, B.3    Xuan, X.4    Fujisaki, K.5
  • 11
    • 0001587857 scopus 로고
    • Digestive enzymes in the American lobster (Homarus americanus)
    • Brockerhoff H, Hoyle RJ, Hwang PC (1970) Digestive enzymes in the American lobster (Homarus americanus). J Fish Res Board Can 27: 1357-1370.
    • (1970) J Fish Res Board Can , vol.27 , pp. 1357-1370
    • Brockerhoff, H.1    Hoyle, R.J.2    Hwang, P.C.3
  • 12
    • 3042830460 scopus 로고    scopus 로고
    • Gene amplification and cold adaptation of pepsin in Antarctic fish: a possible strategy for food digestion at low temperature
    • Carginale V, Trinchella F, Capasso R, Parisia E (2004) Gene amplification and cold adaptation of pepsin in Antarctic fish: a possible strategy for food digestion at low temperature. Gene 336: 195-205.
    • (2004) Gene , vol.336 , pp. 195-205
    • Carginale, V.1    Trinchella, F.2    Capasso, R.3    Parisia, E.4
  • 15
    • 0026806495 scopus 로고
    • Cloning of cDNA for mosquito lysosomal aspartic protease
    • Cho WL, Raikhel AS (1992) Cloning of cDNA for mosquito lysosomal aspartic protease. J Biol Chem 267: 21823-21829.
    • (1992) J Biol Chem , vol.267 , pp. 21823-21829
    • Cho, W.L.1    Raikhel, A.S.2
  • 17
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies DR (1990) The structure and function of the aspartic proteinases. Annu Rev Biophys Biophys Chem 19: 189-215.
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 20
    • 0025641567 scopus 로고
    • The digestive system of the lobster, Homarus americanus: II. Terminal hepatic arterioles of the digestive gland
    • Factor JR, Naar M (1990) The digestive system of the lobster, Homarus americanus: II. Terminal hepatic arterioles of the digestive gland. J Morphol 206: 283-291.
    • (1990) J Morphol , vol.206 , pp. 283-291
    • Factor, J.R.1    Naar, M.2
  • 21
    • 0011288815 scopus 로고
    • Cloning and sequence analysis of cDNA for human cathepsin D
    • Faust PL, Kornfeld S, Chirgwin JM (1985) Cloning and sequence analysis of cDNA for human cathepsin D. Proc Natl Acad Sci USA 82: 4910-4914.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4910-4914
    • Faust, P.L.1    Kornfeld, S.2    Chirgwin, J.M.3
  • 22
    • 0030681366 scopus 로고    scopus 로고
    • Review, psychrophilic enzymes: molecular basis of cold adaptation
    • Feller G, Gerday C (1997) Review, psychrophilic enzymes: molecular basis of cold adaptation. Cell Mol Life Sci 53: 830-841.
    • (1997) Cell Mol Life Sci , vol.53 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 23
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: hot topics in cold adaptation
    • Feller G, Gerday C (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nat Rev Microbiol 1: 200-208.
    • (2003) Nat Rev Microbiol , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 24
    • 33745006609 scopus 로고    scopus 로고
    • Dual role of cathepsin D: ligand and protease
    • Fusek M, Větvička V (2005) Dual role of cathepsin D: ligand and protease. Biomed Papers 149: 43-50.
    • (2005) Biomed Papers , vol.149 , pp. 43-50
    • Fusek, M.1    Větvička, V.2
  • 25
    • 0001284353 scopus 로고
    • Purification, properties and immunoassay of trypsin from Penaeus japonicus
    • Galgani F, Benyamin Y, van Wormhoudt A (1985) Purification, properties and immunoassay of trypsin from Penaeus japonicus. Comp Biochem Physiol B 81: 447-452.
    • (1985) Comp Biochem Physiol B , vol.81 , pp. 447-452
    • Galgani, F.1    Benyamin, Y.2    van Wormhoudt, A.3
  • 26
    • 0027485558 scopus 로고
    • Substrate-gel electrophoresis for composition and molecular weight of proteinases of proteinaceous proteinase inhibitor
    • García-Carreño FL, Dimes LE, Haard N (1993) Substrate-gel electrophoresis for composition and molecular weight of proteinases of proteinaceous proteinase inhibitor. Anal Biochem 214: 65-69.
    • (1993) Anal Biochem , vol.214 , pp. 65-69
    • García-Carreño, F.L.1    Dimes, L.E.2    Haard, N.3
  • 28
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierasch LM (1989) Signal sequences. Biochemistry 28: 923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 29
    • 0028178452 scopus 로고
    • Protein digestion in the European lobster, Homarus gammarus (L.)
    • Glass HJ, Stark JR (1994) Protein digestion in the European lobster, Homarus gammarus (L.). Comp Biochem Physiol 108B: 225-235.
    • (1994) Comp Biochem Physiol , vol.108 B , pp. 225-235
    • Glass, H.J.1    Stark, J.R.2
  • 30
    • 21244469127 scopus 로고    scopus 로고
    • Atlantic cod trypsins: from basic research to practical applications
    • Gudmundsdóttir Á, Pálsdóttir HM (2005) Atlantic cod trypsins: from basic research to practical applications. Mar Biotechnol 7: 77-88.
    • (2005) Mar Biotechnol , vol.7 , pp. 77-88
    • Gudmundsdóttir, Á.1    Pálsdóttir, H.M.2
  • 32
    • 84952490376 scopus 로고
    • A review of proteolytic enzymes from marine organisms and their application in the food industry
    • Haard NF (1991) A review of proteolytic enzymes from marine organisms and their application in the food industry. J Aquat Food Prod Technol 1: 17-35.
    • (1991) J Aquat Food Prod Technol , vol.1 , pp. 17-35
    • Haard, N.F.1
  • 33
    • 0037967590 scopus 로고    scopus 로고
    • A physiological and biochemical model for digestion in the ectoparasitic mite, Psoroptes ovis (Acari: Psoroptidae)
    • Hamilton KA, Nisbet AJ, Lehane MJ, Taylor MA, Billingsley PF (2003) A physiological and biochemical model for digestion in the ectoparasitic mite, Psoroptes ovis (Acari: Psoroptidae). Int J Parasitol 33: 773-785.
    • (2003) Int J Parasitol , vol.33 , pp. 773-785
    • Hamilton, K.A.1    Nisbet, A.J.2    Lehane, M.J.3    Taylor, M.A.4    Billingsley, P.F.5
  • 34
    • 0030567997 scopus 로고    scopus 로고
    • Acasp, a gene encoding a cathepsin D-like aspartic protease from the hookworm Ancylostoma caninum
    • Harrop SA, Prociv P, Brindley PJ (1996) Acasp, a gene encoding a cathepsin D-like aspartic protease from the hookworm Ancylostoma caninum. Biochem Biophys Res Commun 227: 294-302.
    • (1996) Biochem Biophys Res Commun , vol.227 , pp. 294-302
    • Harrop, S.A.1    Prociv, P.2    Brindley, P.J.3
  • 35
    • 0039054095 scopus 로고    scopus 로고
    • Purification and characterization of chymotrypsin from Penaeus vannamei (Crustacea:Decapoda)
    • Hernández-Cortés P, Whitaker JR, García-Carreño FL (1997) Purification and characterization of chymotrypsin from Penaeus vannamei (Crustacea: Decapoda). J Food Biochem 21: 497-514.
    • (1997) J Food Biochem , vol.21 , pp. 497-514
    • Hernández-Cortés, P.1    Whitaker, J.R.2    García-Carreño, F.L.3
  • 36
    • 0344758480 scopus 로고    scopus 로고
    • Trypsin from Pacifastacus leniusculus hepatopancreas: purification and cDNA cloning of the synthesized zymogen
    • Hernández-Cortés P, Cerenius L, García-Carreño FL, Soderhal K (1999) Trypsin from Pacifastacus leniusculus hepatopancreas: purification and cDNA cloning of the synthesized zymogen. Biol Chem 380: 499-501.
    • (1999) Biol Chem , vol.380 , pp. 499-501
    • Hernández-Cortés, P.1    Cerenius, L.2    García-Carreño, F.L.3    Soderhal, K.4
  • 37
    • 0001130158 scopus 로고
    • Digestive enzyme secretion after dietary in the American lobster (Homarus americanus)
    • Hoyle RJ (1973) Digestive enzyme secretion after dietary in the American lobster (Homarus americanus). J Fish Res Board Can 30: 1647-1653.
    • (1973) J Fish Res Board Can , vol.30 , pp. 1647-1653
    • Hoyle, R.J.1
  • 39
    • 33846588294 scopus 로고    scopus 로고
    • Food digestion by cathepsin L and digestion-related rapid cell differentiation in shrimp hepatopancreas
    • Hu KJ, Leung PSC (2007) Food digestion by cathepsin L and digestion-related rapid cell differentiation in shrimp hepatopancreas. Comp Biochem Physiol 146B: 69-80.
    • (2007) Comp Biochem Physiol , vol.146 B , pp. 69-80
    • Hu, K.J.1    Leung, P.S.C.2
  • 40
    • 0036181085 scopus 로고    scopus 로고
    • Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development
    • Kageyama T (2002) Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development. Cell Mol Life Sci 59: 288-306.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 288-306
    • Kageyama, T.1
  • 42
    • 0024971481 scopus 로고
    • Purification and characterization of a digestive cysteine proteinase from the American lobster (Homarus americanus)
    • Laycock MV, Hirama T, Hasnain S, Watson D, Storer A (1989) Purification and characterization of a digestive cysteine proteinase from the American lobster (Homarus americanus). Biochem J 263: 439-444.
    • (1989) Biochem J , vol.263 , pp. 439-444
    • Laycock, M.V.1    Hirama, T.2    Hasnain, S.3    Watson, D.4    Storer, A.5
  • 43
    • 0026001237 scopus 로고
    • Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus)
    • Laycock MV, MacKay RM, Di Fruscio M, Gallant JW (1991) Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus). FEBS Lett 292: 115-120.
    • (1991) FEBS Lett , vol.292 , pp. 115-120
    • Laycock, M.V.1    MacKay, R.M.2    Di Fruscio, M.3    Gallant, J.W.4
  • 44
    • 0032544571 scopus 로고    scopus 로고
    • Cathepsin L gene organization in crustaceans
    • Le Boulay C, Sellos D, van Wormhoudt A (1998) Cathepsin L gene organization in crustaceans. Gene 218: 77-84.
    • (1998) Gene , vol.218 , pp. 77-84
    • Le Boulay, C.1    Sellos, D.2    van Wormhoudt, A.3
  • 45
    • 0036792132 scopus 로고    scopus 로고
    • Expression of hemocyanin and digestive enzyme messenger RNAs in the hepatopancreas of the black tiger shrimp Penaeus monodon
    • Lehnert SH, Johnson SE (2002) Expression of hemocyanin and digestive enzyme messenger RNAs in the hepatopancreas of the black tiger shrimp Penaeus monodon. Comp Biochem Physiol 133B: 163-171.
    • (2002) Comp Biochem Physiol , vol.133 B , pp. 163-171
    • Lehnert, S.H.1    Johnson, S.E.2
  • 46
    • 0005492283 scopus 로고    scopus 로고
    • Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation
    • Leiros HK, Willassen NP, Smalås AO (2000) Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation. Eur J Biochem 267: 1039-1049.
    • (2000) Eur J Biochem , vol.267 , pp. 1039-1049
    • Leiros, H.K.1    Willassen, N.P.2    Smalås, A.O.3
  • 48
    • 84948975658 scopus 로고    scopus 로고
    • Functional morphology of the digestive system
    • B. F. Phillips and J. Kittaka (Eds.), London: Blackwell
    • Mikami S, Takashima F (2000) Functional morphology of the digestive system. In: Phillips BF, Kittaka J (eds) Spiny lobsters: fisheries and culture. Blackwell, London, pp 601-610.
    • (2000) Spiny Lobsters: Fisheries and Culture , pp. 601-610
    • Mikami, S.1    Takashima, F.2
  • 50
    • 33645060389 scopus 로고    scopus 로고
    • Digestion physiology and proteolytic enzymes of crustacean species of the Mexican Pacific Ocean
    • M. E. Hendrickx (Ed.), Mexico City: UNAM
    • Muhlia-Almazán A, García-Carreño FL (2003) Digestion physiology and proteolytic enzymes of crustacean species of the Mexican Pacific Ocean. In: Hendrickx ME (ed) Contributions to the study of east Pacific crustaceans 2. UNAM, Mexico City, pp 77-91.
    • (2003) Contributions to the Study of East Pacific Crustaceans 2 , pp. 77-91
    • Muhlia-Almazán, A.1    García-Carreño, F.L.2
  • 51
    • 37649009347 scopus 로고    scopus 로고
    • Peculiarities of digestive function of proteinases in invertebrates-inhabitants of cold seas
    • Mukhin V, Smirnova E, Novikov V (2007) Peculiarities of digestive function of proteinases in invertebrates-inhabitants of cold seas. J Evol Biochem Physiol 43: 476-482.
    • (2007) J Evol Biochem Physiol , vol.43 , pp. 476-482
    • Mukhin, V.1    Smirnova, E.2    Novikov, V.3
  • 54
    • 0021273620 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurath H (1984) Evolution of proteolytic enzymes. Science 224: 350-357.
    • (1984) Science , vol.224 , pp. 350-357
    • Neurath, H.1
  • 55
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10: 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 56
    • 0035104561 scopus 로고    scopus 로고
    • Studies on digestive proteases from midgut glands of a shrimp, Penaeus indicus, and a lobster, Nephrops norvegicus
    • Omondi J, Stark JR (2001) Studies on digestive proteases from midgut glands of a shrimp, Penaeus indicus, and a lobster, Nephrops norvegicus. Appl Biochem Biotechnol 90: 137-153.
    • (2001) Appl Biochem Biotechnol , vol.90 , pp. 137-153
    • Omondi, J.1    Stark, J.R.2
  • 58
    • 35448999693 scopus 로고    scopus 로고
    • Effect of starvation on global gene expression and proteolysis in rainbow trout (Oncorhynchus mykiss)
    • Salem M, Silverstein J, Rexroad CE, Yao J (2007) Effect of starvation on global gene expression and proteolysis in rainbow trout (Oncorhynchus mykiss). Genomics 8: 328.
    • (2007) Genomics , vol.8 , pp. 328
    • Salem, M.1    Silverstein, J.2    Rexroad, C.E.3    Yao, J.4
  • 63
    • 0035746634 scopus 로고    scopus 로고
    • Enzymes from fish and aquatic invertebrates and their application in the food industry
    • Shahidi F, Janak Kamil YVA (2001) Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci Technol 12: 435-464.
    • (2001) Trends Food Sci Technol , vol.12 , pp. 435-464
    • Shahidi, F.1    Janak Kamil, Y.V.A.2
  • 64
    • 0021140722 scopus 로고
    • Amino acid sequence of porcine spleen cathepsin D
    • Shewale JG, Tang J (1984) Amino acid sequence of porcine spleen cathepsin D. Proc Natl Acad Sci USA 81: 3703-3707.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3703-3707
    • Shewale, J.G.1    Tang, J.2
  • 66
    • 57549115852 scopus 로고    scopus 로고
    • Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases
    • Sojka D, Franta Z, Horn M, Hajdusek O, Caffrey C, Mares M, Kopacek P (2008) Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases. Parasit Vectors 1: 7.
    • (2008) Parasit Vectors , vol.1 , pp. 7
    • Sojka, D.1    Franta, Z.2    Horn, M.3    Hajdusek, O.4    Caffrey, C.5    Mares, M.6    Kopacek, P.7
  • 67
    • 0021099335 scopus 로고
    • Oligosaccharide units of lysosomal cathepsin D from porcine spleen. Amino acid sequence and carbohydrate structure of the glycopeptides
    • Takahashi T, Schmidt PG, Tang J (1983) Oligosaccharide units of lysosomal cathepsin D from porcine spleen. Amino acid sequence and carbohydrate structure of the glycopeptides. J Biol Chem 258: 2819-2830.
    • (1983) J Biol Chem , vol.258 , pp. 2819-2830
    • Takahashi, T.1    Schmidt, P.G.2    Tang, J.3
  • 68
    • 0023209825 scopus 로고
    • Evolution in the structure and function of aspartic proteases
    • Tang J, Wong RNS (1987) Evolution in the structure and function of aspartic proteases. J Cell Biochem 33: 53-63.
    • (1987) J Cell Biochem , vol.33 , pp. 53-63
    • Tang, J.1    Wong, R.N.S.2
  • 69
    • 34848858939 scopus 로고    scopus 로고
    • Regulation of progastrics in mRNA levels in sea bass (Dicentrarchus labrax) in response to fluctuations in food availability
    • Terova G, Rimoldi S, Larghi S, Bernardini G, Gornati R, Saroglia M (2007) Regulation of progastrics in mRNA levels in sea bass (Dicentrarchus labrax) in response to fluctuations in food availability. Biochem Biophys Res Commun 363: 591-596.
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 591-596
    • Terova, G.1    Rimoldi, S.2    Larghi, S.3    Bernardini, G.4    Gornati, R.5    Saroglia, M.6
  • 70
    • 14644439307 scopus 로고    scopus 로고
    • Cysteine proteinases substitute for serine proteinases in the midgut glands of Crangon crangon and Crangon allmani (Decapoda: Caridea)
    • Teschke M, Saborowski R (2005) Cysteine proteinases substitute for serine proteinases in the midgut glands of Crangon crangon and Crangon allmani (Decapoda: Caridea). J Exp Mar Biol Ecol 315: 213-299.
    • (2005) J Exp Mar Biol Ecol , vol.315 , pp. 213-299
    • Teschke, M.1    Saborowski, R.2
  • 71
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res 22: 4673-4680.
    • (1994) Nucleic Acid Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 73
    • 0032529137 scopus 로고    scopus 로고
    • The structures of asparagine-linked oligosaccharides of rat liver cathepsin L reflect the substrate specificity of lysosomal α-mannosidase
    • Towatari T, Miyamura T, Kondo A, Kato I, Inoue M, Yano M, Kido H (1998) The structures of asparagine-linked oligosaccharides of rat liver cathepsin L reflect the substrate specificity of lysosomal α-mannosidase. Eur J Biochem 256: 163-169.
    • (1998) Eur J Biochem , vol.256 , pp. 163-169
    • Towatari, T.1    Miyamura, T.2    Kondo, A.3    Kato, I.4    Inoue, M.5    Yano, M.6    Kido, H.7
  • 74
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne G (1990) The signal peptide. J Membr Biol 115: 195-201.
    • (1990) J Membr Biol , vol.115 , pp. 195-201
    • von Heijne, G.1


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