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Volumn 6, Issue 3, 1997, Pages 228-237

Amylase in Pecten maximus (mollusca, bivalves): Protein and cDNA characterization; quantification of the expression in the digestive gland

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; COMPLEMENTARY DNA; MESSENGER RNA; STARCH;

EID: 0031239031     PISSN: 10536426     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 0019360101 scopus 로고
    • Evolution of the cytochrome c investigating the maximum parsimony method
    • Baba, M.L., Darga, L.L., Goodman, M., and Czelusniah, J. (1981). Evolution of the cytochrome c investigating the maximum parsimony method. J Mol Evol 17:197-213.
    • (1981) J Mol Evol , vol.17 , pp. 197-213
    • Baba, M.L.1    Darga, L.L.2    Goodman, M.3    Czelusniah, J.4
  • 3
    • 0023047173 scopus 로고
    • The α-amylase gene in Drosophila melanogaster, nucleotide sequence, gene structure and expression
    • Boer, P.M., and Hickey, D.A. (1986). The α-amylase gene in Drosophila melanogaster, nucleotide sequence, gene structure and expression. Nucleic Acid Res 14:8399-8411.
    • (1986) Nucleic Acid Res , vol.14 , pp. 8399-8411
    • Boer, P.M.1    Hickey, D.A.2
  • 4
    • 0011190524 scopus 로고
    • Environmental control of amylase phenotype in amphipods of the genus
    • Borowsky, R. (1984). Environmental control of amylase phenotype in amphipods of the genus Gammarus Biol Bull 167:647-657.
    • (1984) Gammarus Biol Bull , vol.167 , pp. 647-657
    • Borowsky, R.1
  • 5
    • 0343958722 scopus 로고
    • Dynamique et enzymologie de la digestion chez l'huitre Crassostrea gigas (Thunberg)
    • Montpellier, France: Bases biologiques de l'aquaculture
    • Boucaud-Camou, E., Lebesnerais, C., Lubet, P., and Lihrmann, I. (1983). Dynamique et enzymologie de la digestion chez l'huitre Crassostrea gigas (Thunberg). In: Ifremer, Actes de colloques. Montpellier, France: Bases biologiques de l'aquaculture, 1:75-96.
    • (1983) Ifremer, Actes de Colloques , vol.1 , pp. 75-96
    • Boucaud-Camou, E.1    Lebesnerais, C.2    Lubet, P.3    Lihrmann, I.4
  • 6
    • 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. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 7
    • 0018639079 scopus 로고
    • Isolation of biologicaly active ribonucleic acid from sources enriched in ribonucleases
    • Chirgwin, J.J., Przbyla, A.E., Mac Donald, R.J., and Rutter, W.J. (1979). Isolation of biologicaly active ribonucleic acid from sources enriched in ribonucleases Biochemistry 18:5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.J.1    Przbyla, A.E.2    Mac Donald, R.J.3    Rutter, W.J.4
  • 8
    • 0017756085 scopus 로고
    • Different action of hormonal stimulation on the biosynthesis of three pancreatic enzymes
    • Dagorn, J.C., and Mongeau, R. (1977). Different action of hormonal stimulation on the biosynthesis of three pancreatic enzymes. Biochim Biophys Acta 498:76-82.
    • (1977) Biochim Biophys Acta , vol.498 , pp. 76-82
    • Dagorn, J.C.1    Mongeau, R.2
  • 9
    • 0019796350 scopus 로고
    • Dietary regulation of pancreatic protein synthesis, I: Rapid specific modulation of enzyme synthesis by changes in dietary composition
    • Dagorn, J.C., and Lahaie, R.G. (1981). Dietary regulation of pancreatic protein synthesis, I: rapid specific modulation of enzyme synthesis by changes in dietary composition. Biochim Biophys Acta 654:111-118.
    • (1981) Biochim Biophys Acta , vol.654 , pp. 111-118
    • Dagorn, J.C.1    Lahaie, R.G.2
  • 10
    • 0026624828 scopus 로고
    • Multiple analysis genes in Drosophila ananassae and related species
    • Da Lage, J.L., Lemeunier, F., Cariou, M.L., and David, J.R. (1992). Multiple analysis genes in Drosophila ananassae and related species. Genet Res 59:85-92.
    • (1992) Genet Res , vol.59 , pp. 85-92
    • Da Lage, J.L.1    Lemeunier, F.2    Cariou, M.L.3    David, J.R.4
  • 11
    • 78651153791 scopus 로고
    • Disc electrophoresis, II: Method and application to human serum proteins
    • Davis, B.T. (1964). Disc electrophoresis, II: method and application to human serum proteins. Ann N Y Acad Sci 321:404-428.
    • (1964) Ann N Y Acad Sci , vol.321 , pp. 404-428
    • Davis, B.T.1
  • 12
    • 0342652707 scopus 로고
    • Influence of the composition of the diet on the enzyme content of rat pancreas
    • De Reuck A.V.S, and Cameron, M.P. (eds). Boston, Mass.: Little, Brown
    • Desnuelle, P., Reboud, J.P., and Ben Abdeljlil, A. (1962). Influence of the composition of the diet on the enzyme content of rat pancreas. In: De Reuck A.V.S, and Cameron, M.P. (eds). Ciba Foundation Symposium on the Exocrine Pancreas. Boston, Mass.: Little, Brown, 90-114.
    • (1962) Ciba Foundation Symposium on the Exocrine Pancreas , pp. 90-114
    • Desnuelle, P.1    Reboud, J.P.2    Ben Abdeljlil, A.3
  • 13
    • 0025053917 scopus 로고
    • BISANCE, French service for access to biomolecular sequence databases
    • Dessen, P., Fondrat, C., Valencien, C., and Mugnier, C. (1990). BISANCE, French service for access to biomolecular sequence databases. Comput Appl Biosci 6:355-356.
    • (1990) Comput Appl Biosci , vol.6 , pp. 355-356
    • Dessen, P.1    Fondrat, C.2    Valencien, C.3    Mugnier, C.4
  • 14
    • 0029109387 scopus 로고
    • In vitro investigation of α-amylase release from the digestive cells of the bivalve mollusc Pecten maximus, effect of second messengers and biogenic amines
    • Giard, W., Favrel, P., and Boucaud-Camou, E. (1995). In vitro investigation of α-amylase release from the digestive cells of the bivalve mollusc Pecten maximus, effect of second messengers and biogenic amines. J Comp Physiol B 164:518-523.
    • (1995) J Comp Physiol B , vol.164 , pp. 518-523
    • Giard, W.1    Favrel, P.2    Boucaud-Camou, E.3
  • 15
    • 0027179572 scopus 로고
    • Molluscan chymotrypsin-like protease, structure, localization and substrate specificity
    • Groppe, J.C., and Morse, D.E. (1993a). Molluscan chymotrypsin-like protease, structure, localization and substrate specificity. Arch Biochem Biophys 305:159-169.
    • (1993) Arch Biochem Biophys , vol.305 , pp. 159-169
    • Groppe, J.C.1    Morse, D.E.2
  • 16
    • 0027161297 scopus 로고
    • Isolation of a full-length RNA templates for reverse transcription from tissues rich in RNAse and proteoglycans
    • Groppe, J.C., and Morse, D.E. (1993b). Isolation of a full-length RNA templates for reverse transcription from tissues rich in RNAse and proteoglycans. Anal Biochem 210:337-343.
    • (1993) Anal Biochem , vol.210 , pp. 337-343
    • Groppe, J.C.1    Morse, D.E.2
  • 17
    • 0027752188 scopus 로고
    • The salivary gland of the vector mosquito Aedes aegypti express a novel member of the amylase gene family
    • Grossman, G.L., and James, A.A. (1993). The salivary gland of the vector mosquito Aedes aegypti express a novel member of the amylase gene family. Insect Mol Biol 1:223-232.
    • (1993) Insect Mol Biol , vol.1 , pp. 223-232
    • Grossman, G.L.1    James, A.A.2
  • 18
    • 0025342577 scopus 로고
    • Unified approach to alignment and phylogenies
    • Hein, J. (1990). Unified approach to alignment and phylogenies. Methods Enzymol 183:624-644.
    • (1990) Methods Enzymol , vol.183 , pp. 624-644
    • Hein, J.1
  • 19
    • 0027306097 scopus 로고
    • The amylase secreting cells of the stomach of the scallop, Pecten maximus, ultrastructural, immunohistochemical and immunocytochemical characterizations
    • Henry, M., Benlimane, N., Boucaud-Camou, E., Mathieu, M., Donval, A., and Van Wormhoudt, A. (1993). The amylase secreting cells of the stomach of the scallop, Pecten maximus, ultrastructural, immunohistochemical and immunocytochemical characterizations. Tissue Cell 25:537-548.
    • (1993) Tissue Cell , vol.25 , pp. 537-548
    • Henry, M.1    Benlimane, N.2    Boucaud-Camou, E.3    Mathieu, M.4    Donval, A.5    Van Wormhoudt, A.6
  • 20
    • 0027082157 scopus 로고
    • New conserved aminoacid region of α-amylase in the third loop of their (β/α) 8 barrel domain
    • Janecek, S. (1992). New conserved aminoacid region of α-amylase in the third loop of their (β/α) 8 barrel domain. Biochem J 288:1069-1075.
    • (1992) Biochem J , vol.288 , pp. 1069-1075
    • Janecek, S.1
  • 21
    • 0028021627 scopus 로고
    • Sequence similarities and evolutionary relationships of microbobial, plant and animal α-amylases
    • Janecek, S. (1994). Sequence similarities and evolutionary relationships of microbobial, plant and animal α-amylases. Eur J Biochem 224:519-524.
    • (1994) Eur J Biochem , vol.224 , pp. 519-524
    • Janecek, S.1
  • 22
    • 0026496222 scopus 로고
    • The levels of lactase and sucrase-isomaltase along the rabbit small intestine are regulated both at the mRNA level and post-translationally
    • Keller, P., Zwicker, E., Mantei, N., and Semenza, G. (1992). The levels of lactase and sucrase-isomaltase along the rabbit small intestine are regulated both at the mRNA level and post-translationally. FEBS Lett 313:265-269.
    • (1992) FEBS Lett , vol.313 , pp. 265-269
    • Keller, P.1    Zwicker, E.2    Mantei, N.3    Semenza, G.4
  • 23
    • 0020475449 scopus 로고
    • A single method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982). A single method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 24
    • 0019795914 scopus 로고
    • Pancreatic islet-acinar cell interaction, amylase messenger RNA levels are determined by insulin
    • Korc, M., Owerbach, D., Quinto, C., and Rutter, W.J. (1981). Pancreatic islet-acinar cell interaction, amylase messenger RNA levels are determined by insulin. Science 213:351-353.
    • (1981) Science , vol.213 , pp. 351-353
    • Korc, M.1    Owerbach, D.2    Quinto, C.3    Rutter, W.J.4
  • 25
    • 0028042224 scopus 로고
    • Adaptation of digestive enzymes to dietary protein, carbohydrate and fibre levels and influence of protein and carbohydrate quality in Pennaeus vannamei larvae (Crustacea, Decapoda)
    • Le Moullac, G., Van Wormhoudt, A., and Aquacop. (1994). Adaptation of digestive enzymes to dietary protein, carbohydrate and fibre levels and influence of protein and carbohydrate quality in Pennaeus vannamei larvae (Crustacea, Decapoda). Aquat Living Resourc 7:203-210.
    • (1994) Aquat Living Resourc , vol.7 , pp. 203-210
    • Le Moullac, G.1    Van Wormhoudt, A.2
  • 28
    • 0010294220 scopus 로고
    • Carbohydrate digestion in Ostrea edulis L
    • Mathers, N.F. (1973). Carbohydrate digestion in Ostrea edulis L. Proc Malac Soc 40:359-367.
    • (1973) Proc Malac Soc , vol.40 , pp. 359-367
    • Mathers, N.F.1
  • 29
    • 0017912702 scopus 로고
    • α-Amylase from human pancreatic juice as an electrophoretically pure isozyme
    • Matsuura, K., Ogawa, M., Kosaki, G., Minamiura, N., and Yamamoto, T. (1978). α-Amylase from human pancreatic juice as an electrophoretically pure isozyme. J Biochem 83:329-332.
    • (1978) J Biochem , vol.83 , pp. 329-332
    • Matsuura, K.1    Ogawa, M.2    Kosaki, G.3    Minamiura, N.4    Yamamoto, T.5
  • 31
    • 0022670999 scopus 로고
    • Nucleotide sequence of the Bacillus stearohermophilus α-amylase gene
    • Nakajima, R., Imanaka, J., and Aiba, S. (1986). Nucleotide sequence of the Bacillus stearohermophilus α-amylase gene. Appl Microbiol Biotechnol 23:355-360.
    • (1986) Appl Microbiol Biotechnol , vol.23 , pp. 355-360
    • Nakajima, R.1    Imanaka, J.2    Aiba, S.3
  • 33
    • 0002550145 scopus 로고
    • A possible role of α-amylase isoenzymes from the style of the mussel Chloromytilus meridionalis (Krauss) following thermal acclimation
    • Newell, R.C., Parker, I., and Cook, P.A. (1980). A possible role of α-amylase isoenzymes from the style of the mussel Chloromytilus meridionalis (Krauss) following thermal acclimation. J Exp Mar Biol Ecol 47:1-8.
    • (1980) J Exp Mar Biol Ecol , vol.47 , pp. 1-8
    • Newell, R.C.1    Parker, I.2    Cook, P.A.3
  • 34
    • 0022629141 scopus 로고
    • Complete amino-acid sequence and location of the five disulfide bridges in porcine pancreatic α-amylases
    • Pasero, L., Mazzei-Pierron, Y., Abadie, B., Chicheportiche, Y., and Marchis-Mouren, G. (1986). Complete amino-acid sequence and location of the five disulfide bridges in porcine pancreatic α-amylases. Biochim Biophys Acta 869: 147-157.
    • (1986) Biochim Biophys Acta , vol.869 , pp. 147-157
    • Pasero, L.1    Mazzei-Pierron, Y.2    Abadie, B.3    Chicheportiche, Y.4    Marchis-Mouren, G.5
  • 35
    • 0343958716 scopus 로고
    • Biological activity of biosynthetic rainbow trout growth hormone in the eastern oyster, Crassostrea gigas
    • Paynter, K.T., and Chen, T.T. (1991). Biological activity of biosynthetic rainbow trout growth hormone in the eastern oyster, Crassostrea gigas. Biol Bull 181:459-462.
    • (1991) Biol Bull , vol.181 , pp. 459-462
    • Paynter, K.T.1    Chen, T.T.2
  • 37
    • 0024384836 scopus 로고
    • Hydrophobic cluster analysis of the primary sequences of α-amylases
    • Raimbaud, E., Buleon, A., Perez, S., and Henrissat, B. (1992). Hydrophobic cluster analysis of the primary sequences of α-amylases. Int J Biol Macromol 11:217-225.
    • (1992) Int J Biol Macromol , vol.11 , pp. 217-225
    • Raimbaud, E.1    Buleon, A.2    Perez, S.3    Henrissat, B.4
  • 38
    • 0019123050 scopus 로고
    • Structure of a family of rat amylase genes
    • Rutter, WJ. (1980). Structure of a family of rat amylase genes. Nature 287:117-122.
    • (1980) Nature , vol.287 , pp. 117-122
    • Rutter, W.J.1
  • 39
    • 0010321206 scopus 로고
    • Trypsine, amylase et prot́eines du zooplancton, dosage automatique et manuel
    • Samain, J.F., Daniel, J.Y., Le Coz, J.R. (1977). Trypsine, amylase et prot́eines du zooplancton, dosage automatique et manuel. J Exp Mar Biol Ecol 29:279-289.
    • (1977) J Exp Mar Biol Ecol , vol.29 , pp. 279-289
    • Samain, J.F.1    Daniel, J.Y.2    Le Coz, J.R.3
  • 41
    • 84913158896 scopus 로고
    • Amylases in Mytilus edulis (Mollusca Pteriomorpha), ein nachweis zweir polymorph system
    • Sanger, R., and Hagenmaier, H.E. (1986). Amylases in Mytilus edulis (Mollusca Pteriomorpha), ein nachweis zweir polymorph system. Zool Anz 217:116-118.
    • (1986) Zool Anz , vol.217 , pp. 116-118
    • Sanger, R.1    Hagenmaier, H.E.2
  • 42
    • 0343522865 scopus 로고
    • Amylases in Dreissena polymorpha Pall (Mollusca, Eulamellibranchiata), evidence for two polymorphic systems
    • Scheil, H.G., and Guenther, A. (1981). Amylases in Dreissena polymorpha Pall (Mollusca, Eulamellibranchiata), evidence for two polymorphic systems. Zool Anz 207:3-4.
    • (1981) Zool Anz , vol.207 , pp. 3-4
    • Scheil, H.G.1    Guenther, A.2
  • 43
    • 0002565780 scopus 로고
    • Adjustment of the activity of α-amylase extracted from the style of the black mussel Choromytilus meridionalis (Krauss) in response to thermal acclimatation
    • Seiderer, L.J., and Newell, R.C. (1979). Adjustment of the activity of α-amylase extracted from the style of the black mussel Choromytilus meridionalis (Krauss) in response to thermal acclimatation. J Exp Mar Biol Ecol 39:79-86.
    • (1979) J Exp Mar Biol Ecol , vol.39 , pp. 79-86
    • Seiderer, L.J.1    Newell, R.C.2
  • 44
    • 0026760832 scopus 로고
    • Molecular cloning of a c-DNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimp Penaeus vannamei (Crustacea, Decapoda)
    • Sellos, D., and Van Wormhoudt, A. (1992). Molecular cloning of a c-DNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimp Penaeus vannamei (Crustacea, Decapoda). FEBS Lett, 309:219-224.
    • (1992) FEBS Lett , vol.309 , pp. 219-224
    • Sellos, D.1    Van Wormhoudt, A.2
  • 45
    • 0000981886 scopus 로고
    • Carbohydrate digestion in Pecten maximus
    • Stark, J.R., and Walker, R.S. (1983). Carbohydrate digestion in Pecten maximus. Comp Biochem Physiol 76B:173-177.
    • (1983) Comp Biochem Physiol , vol.76 B , pp. 173-177
    • Stark, J.R.1    Walker, R.S.2
  • 46
    • 0025076887 scopus 로고
    • Preliminary report on the digestive enzymes present in the digestive gland of Perna viridis
    • Teo, L.H., and Sabapathy, V. (1990). Preliminary report on the digestive enzymes present in the digestive gland of Perna viridis. Mar Biol 106:403-407.
    • (1990) Mar Biol , vol.106 , pp. 403-407
    • Teo, L.H.1    Sabapathy, V.2
  • 47
    • 0029889844 scopus 로고
    • Molecular cloning and sequencing of three cDNAs that encode amylase in the hepatopancreas of the shrimp Penaeus vannaemei
    • Van Wormhoudt, A., and Sellos, D. (1995). Molecular cloning and sequencing of three cDNAs that encode amylase in the hepatopancreas of the shrimp Penaeus vannaemei. J Mol Evol 42:543-551.
    • (1995) J Mol Evol , vol.42 , pp. 543-551
    • Van Wormhoudt, A.1    Sellos, D.2
  • 48
    • 0001521885 scopus 로고
    • Amylase polymorphism in crustacea decapoda, electrophoretic and immune-logical studies
    • Van Wormhoudt, A., Bourreau, G., and Le Moullac, G. (1995). Amylase polymorphism in crustacea decapoda, electrophoretic and immune-logical studies. Biochem Systematics Ecol 23:139-149.
    • (1995) Biochem Systematics Ecol , vol.23 , pp. 139-149
    • Van Wormhoudt, A.1    Bourreau, G.2    Le Moullac, G.3
  • 49
    • 0014690791 scopus 로고
    • The relationship of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis
    • Weber, K., and Osborne, M. (1969). The relationship of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis. J Biol Chem 244:4406-4412.
    • (1969) J Biol Chem , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborne, M.2
  • 50
    • 0017049366 scopus 로고
    • Purification d'α-amylases par chromatographie d'affinité sur amidon ŕeticuĺe
    • Weber, M., Foglietti, M-J., and Percheron, F. (1976). Purification d'α-amylases par chromatographie d'affinité sur amidon ŕeticuĺe. Biochimie 58:1299-1302.
    • (1976) Biochimie , vol.58 , pp. 1299-1302
    • Weber, M.1    Foglietti, M.-J.2    Percheron, F.3


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