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Volumn 11, Issue , 2011, Pages

Cloning and expression analysis of the Bombyx mori !-amylase gene (Amy) from the Indigenous Thai silkworm Strain, Nanglai

Author keywords

Amy; Bombyx mori; GAL4 UAS; silkworm

Indexed keywords

BOMBYCIDAE; BOMBYX MORI; HEXAPODA; LEPIDOPTERA; MAMMALIA;

EID: 79955554936     PISSN: None     EISSN: 15362442     Source Type: Journal    
DOI: 10.1673/031.011.0138     Document Type: Article
Times cited : (22)

References (40)
  • 1
    • 0011361213 scopus 로고
    • Biochemical studies of amylases in the silkworm, Bombyx mori L., comparative analysis in diapausing and nondiausing strains
    • Abraham EG, Nagaraju J, Datta RK. 1992. Biochemical studies of amylases in the silkworm, Bombyx mori L., comparative analysis in diapausing and nondiausing strains. Insect Biochemistry and Molecular Biology 22: 867-873.
    • (1992) Insect Biochemistry and Molecular Biology , vol.22 , pp. 867-873
    • Abraham, E.G.1    Nagaraju, J.2    Datta, R.K.3
  • 2
    • 79955553992 scopus 로고
    • Polymorphism of digestive amylase isozyme in the silkworm, Bombyx mori
    • Asakawa H, Hamano K. 1989. Polymorphism of digestive amylase isozyme in the silkworm, Bombyx mori. The Journal of Sericultural Science of Japan 58: 322-326.
    • (1989) The Journal of Sericultural Science of Japan , vol.58 , pp. 322-326
    • Asakawa, H.1    Hamano, K.2
  • 3
    • 0030919607 scopus 로고    scopus 로고
    • Cloning and expression of a chicken α-amylase gene
    • DOI 10.1016/S0378-1119(97)00102-9, PII S0378111997001029
    • Benkel BF, Nguyen T, Ahluwalia N, Benkel K, Hickey DA. 1997. Cloning and expression of a chicken alpha-amylase gene. Gene 192: 261-270. (Pubitemid 27268251)
    • (1997) Gene , vol.192 , Issue.2 , pp. 261-270
    • Benkel, B.F.1    Nguyen, T.2    Ahluwalia, N.3    Benkel, K.I.4    Hickey, D.A.5
  • 4
    • 0023047173 scopus 로고
    • The alphaamylase gene in Drosophila melanogaster: Nucleotide sequence, gene structure and expression motifs
    • Boer PA, Hickey DA. 1987. The alphaamylase gene in Drosophila melanogaster: nucleotide sequence, gene structure and expression motifs. Nucleic Acids Research 14: 8399-8411.
    • (1987) Nucleic Acids Research , vol.14 , pp. 8399-8411
    • Boer, P.A.1    Hickey, D.A.2
  • 5
    • 0030049028 scopus 로고    scopus 로고
    • Variation in sex, stage and tissue-specific expression of the amylase genes in Drosophila ananassae
    • Da Lage JL, Klarenberg A, Cariou M-L. 1996. Variation in sex, stage and tissue-specific expression of the amylase genes in Drosophila ananassae. Heredity 76: 9-18.
    • (1996) Heredity , vol.76 , pp. 9-18
    • Da Lage, J.L.1    Klarenberg, A.2    Cariou, M.-L.3
  • 9
    • 0027752188 scopus 로고
    • The salivary glands of the vector mosquito, Aedes aegypti, express a novel member of the amylase gene family
    • Grossman GL, James AA. 1993. The salivary glands of the vector mosquito, Aedes aegypti, express a novel member of the amylase gene family. Insect Molecular Biology 1: 223-232.
    • (1993) Insect Molecular Biology , vol.1 , pp. 223-232
    • Grossman, G.L.1    James, A.A.2
  • 10
    • 0031200982 scopus 로고    scopus 로고
    • Evidence for two distinct members of the amylase gene family in the yellow fever mosquito, Aedes aegypti
    • DOI 10.1016/S0965-1748(97)00063-5, PII S0965174897000635
    • Grossman GL, Campos Y, Severson DW. James AA. 1997. Evidence for two distinct members of the amylase gene family in the yellow fever mosquito, Aedes aegypti. Insect Biochemistry and Molecular Biology 27: 769-781. (Pubitemid 28075564)
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , Issue.8-9 , pp. 769-781
    • Grossman, G.L.1    Campos, Y.2    Severson, D.W.3    James, A.A.4
  • 11
    • 15944374849 scopus 로고    scopus 로고
    • In vitro analysis of the digestive enzymes amylase and α-glucosidase in the midguts of Locusta migratoria L. in response to the myosuppressin, SchistoFLRFamide
    • DOI 10.1016/j.jinsphys.2004.10.003
    • Hill SR, Orchard I. 2005. In vitro analysis of the digestive enzymes amylase and α- glucosidase in the midgets of α- glucosidase in the midgets of Locusta migratoria L. in response to myosuppressin, SchistoFLRFamide. Journal of Insect Physiology 51: 1-9. (Pubitemid 40427907)
    • (2005) Journal of Insect Physiology , vol.51 , Issue.1 , pp. 1-9
    • Hill, S.R.1    Orchard, I.2
  • 12
    • 0023572287 scopus 로고
    • Primary structure of human pancreatic α-amylase gene: Its comparison with human salivary α-amylase gene
    • DOI 10.1016/0378-1119(87)90213-7
    • Horii A, Emi M, Tomita N, Nishide T, Ogawa M, Mori T, Matsubara K. 1987. Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene. Gene 60: 57-64. (Pubitemid 18026829)
    • (1987) Gene , vol.60 , Issue.1 , pp. 57-64
    • Horii, A.1    Emi, M.2    Tomita, N.3    Nishide, T.4    Ogawa, M.5    Mori, T.6    Matsubara, K.7
  • 13
    • 0347622766 scopus 로고    scopus 로고
    • Targeted Gene Expression Using the GAL4/UAS System in the Silkworm Bombyx mori
    • Imamura M, Nakai J, Inoue S, Quan GX, Kanda T, Tamura T. 2003. Targeted gene expression using the Gal4/UAS system in the silkworm Bombyx mori. Genetics 165: 1329-1340. (Pubitemid 38020253)
    • (2003) Genetics , vol.165 , Issue.3 , pp. 1329-1340
    • Imamura, M.1    Nakai, J.2    Inoue, S.3    Quan, G.X.4    Kanda, T.5    Tamura, T.6
  • 14
    • 0027497395 scopus 로고
    • 8-barrel enzymes revealed by conserved regions of α-amylase
    • DOI 10.1016/0014-5793(93)81729-J
    • Janecek S. 1993. Sequence similarities in (α/α) 8-barrel enzymes reveals by observed regions of α-amylase. FEBS 316: 23-26. (Pubitemid 23029200)
    • (1993) FEBS Letters , vol.316 , Issue.1 , pp. 23-26
    • Janecek, S.1
  • 15
    • 0030778420 scopus 로고    scopus 로고
    • α-Amylase family: Molecular biology and evolution
    • DOI 10.1016/S0079-6107(97)00015-1, PII S0079610797000151
    • Janecek S. 1997. α/β-amylase family: molecular biology and evolution. Progress in Biophysics and Molecular Biology 67: 67-97. (Pubitemid 27491749)
    • (1997) Progress in Biophysics and Molecular Biology , vol.67 , Issue.1 , pp. 67-97
    • Janecek, S.1
  • 16
    • 84996343216 scopus 로고
    • Amylase in the digestive juice of silkworm larvae, Bombyx mori
    • Kanekatsu R. 1972. Amylase in the digestive juice of silkworm larvae, Bombyx mori. The Journal of Sericultural Science of Japan 41: 445-451.
    • (1972) The Journal of Sericultural Science of Japan , vol.41 , pp. 445-451
    • Kanekatsu, R.1
  • 17
    • 0011363827 scopus 로고
    • Studies on further properties for an alkaline amylase in the digestive juice of silkworm, Bombyx mori
    • Kanakatsu R. 1978. Studies on further properties for an alkaline amylase in the digestive juice of silkworm, Bombyx mori. Journal of the Faculty of Textile Science and Technology 76: 1-21.
    • (1978) Journal of the Faculty of Textile Science and Technology , vol.76 , pp. 1-21
    • Kanakatsu, R.1
  • 18
    • 36249025623 scopus 로고    scopus 로고
    • Development of a new piggyBac vector for generating transgenic silkworms using the kynurenine 3-mono oxygenase gene
    • Kobayashi I, Uchino K, Sezutsu H, Iizuka T, Tamura T. 2007. Development of a new piggyBac vector for generating transgenic silkworms using the kynurenine 3-mono oxygenase gene. Journal of Insect Biotechnology and Sericology 76: 145-148. (Pubitemid 350123994)
    • (2007) Journal of Insect Biotechnology and Sericology , vol.76 , Issue.3 , pp. 145-148
    • Kobayashi, I.1    Uchino, K.2    Sezutsu, H.3    Iizuka, T.4    Tamura, T.5
  • 19
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S, Tamura K. Nei M. 2004. MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Bioinformatics 5: 150-163.
    • (2004) Bioinformatics , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 20
    • 79955560760 scopus 로고
    • Genetics of four types of amylases in the silkworm, Bombyx mori
    • Matsumura S. 1933. Genetics of four types of amylases in the silkworm, Bombyx mori. The Journal of Sericultural Science of Japan 4: 168-170.
    • (1933) The Journal of Sericultural Science of Japan , vol.4 , pp. 168-170
    • Matsumura, S.1
  • 24
    • 0005134824 scopus 로고    scopus 로고
    • Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honeybee (Apis mellifera L.)
    • DOI 10.1046/j.1432-1327.1999.00696.x
    • Ohashi K, Natori S, Kubo T. 1999. Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honeybee (Apis mellifera L.). European Journal of Biochemistry 265: 127-133. (Pubitemid 29466020)
    • (1999) European Journal of Biochemistry , vol.265 , Issue.1 , pp. 127-133
    • Ohashi, K.1    Natori, S.2    Kubo, T.3
  • 25
    • 12344263817 scopus 로고    scopus 로고
    • Comparative analysis of the development of the mandibular salivary glands and the labial silk glands in the mulberry silkworm, Bombyx mori
    • DOI 10.1016/j.modgep.2004.10.006, PII S1567133X04001711
    • Parthasarathy R, Gopinathan KP. 2005. Comparative analysis of the development of the mandibular salivary glands and the labial silk glands in the mulberry silkworm, Bombyx mori. Gene Expression Patterns 5: 323-339. (Pubitemid 40124547)
    • (2005) Gene Expression Patterns , vol.5 , Issue.3 , pp. 323-339
    • Parthasarathy, R.1    Gopinathan, K.P.2
  • 26
    • 79955566598 scopus 로고
    • Amylase of the polyvoltine silkworm (Bombyx mori): Variation of activity in the Thai local race
    • Promboon A, Engkakul A, Ngernsiri L, Saksoong P. 1993. Amylase of the polyvoltine silkworm (Bombyx mori): variation of activity in the Thai local race. Sericologia 33: 603-609.
    • (1993) Sericologia , vol.33 , pp. 603-609
    • Promboon, A.1    Engkakul, A.2    Ngernsiri, L.3    Saksoong, P.4
  • 27
    • 0028198814 scopus 로고
    • The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-A resolution
    • DOI 10.1021/bi00186a031
    • Qian M, Haser R, Buisson G, Duee E, Payan F. 1994. The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2 ! resolution. Biochemmistry 33: 6284-6294. (Pubitemid 24190783)
    • (1994) Biochemistry , vol.33 , Issue.20 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 28
    • 14644394911 scopus 로고    scopus 로고
    • Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic α-amylase
    • DOI 10.1021/bi048201t
    • Qian M, Ajandouz EH, Payan F, Nahoum V. 2005. Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic α-Amylase. Biochemistry 44: 3194-3201. (Pubitemid 40321992)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3194-3201
    • Qian, M.1    Ajandouz, E.H.2    Payan, F.3    Nahoum, V.4
  • 29
    • 33746700795 scopus 로고    scopus 로고
    • Characterization of BGTG-1, a tergal gland-secreted alpha-amylase, from the German cockroach, Blattella germanica (L.)
    • DOI 10.1111/j.1365-2583.2006.00652.x
    • Saltzmann KD, Saltzmann KA, Neal JJ, Scharf ME, Bennett GW. 2006. Characterization of BGTG-1, a tergal glandsecreted alpha-amylase, from the German cockroach, Blattella germanica (L.). Insect Molecular Biology 15: 425-433. (Pubitemid 44166564)
    • (2006) Insect Molecular Biology , vol.15 , Issue.4 , pp. 425-433
    • Saltzmann, K.D.1    Saltzmann, K.A.2    Neal, J.J.3    Scharf, M.E.4    Bennett, G.W.5
  • 30
    • 0346857920 scopus 로고    scopus 로고
    • Structure of the of α-amylase genes in crustaceans and molluscs: Evolution of the exon/intron organization
    • Sellos DY, Van Wormhoudt A. 2002. Structure of the of α-amylase genes in crustaceans and molluscs: evolution of the exon/intron organization. Biologia, Bratislava 57 (Suppl. 11): 191-196. (Pubitemid 135713706)
    • (2002) Biologia - Section Cellular and Molecular Biology , vol.57 , Issue.SUPPL. 11 , pp. 191-196
    • Sellos, D.Y.1    Van Wormhoudt, A.2
  • 31
    • 0142025336 scopus 로고    scopus 로고
    • Structure of amylase genes in populations of pacific cupped oyster (Crassostrea gigas): Tissue expression and allelic polymorphism
    • DOI 10.1007/s10126-002-0089-7
    • Sellos DY, Moal J, Degremont L, Huvet A, Daniel J-Y, Nicoulaud S, Boudry P, Samain JF, Wormhoudt AV. 2003. Structure of amylase genes in populations of pacific cupped oyster (Crassostrea gigas): tissue expression and allelic polymorphism. Marine Biotechnology 5: 360-372. (Pubitemid 37293203)
    • (2003) Marine Biotechnology , vol.5 , Issue.4 , pp. 360-372
    • Sellos, D.1    Moal, J.2    Degremont, L.3    Huvet, A.4    Daniel, J.-Y.5    Nicoulaud, S.6    Boudry, P.7    Samain, J.-F.8    Van Wormhoudt, A.9
  • 32
    • 0342378173 scopus 로고    scopus 로고
    • The α-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis
    • DOI 10.1016/S0014-5793(97)00451-1, PII S0014579397004511
    • Strobl S, Gomis-Ruth FX, Maskos K, Frank G, Huber R, Glockshuber R. 1997. The α- amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis. FEBS Letters 409: 109-114. (Pubitemid 27248577)
    • (1997) FEBS Letters , vol.409 , Issue.1 , pp. 109-114
    • Strobl, S.1    Gomis-Ruth, F.-X.2    Maskos, K.3    Frank, G.4    Huber, R.5    Glockshuber, R.6
  • 34
    • 0023841829 scopus 로고
    • Regional distant sequence homology between amylase, α-glucosidase and transglucanosylases
    • Svennson B. 1988. Regional distant sequence homology between amylase, α-glucosidase and transglucanosylases. FEBS Letters 236: 72-76.
    • (1988) FEBS Letters , vol.236 , pp. 72-76
    • Svennson, B.1
  • 38
    • 0029889844 scopus 로고    scopus 로고
    • Cloning and sequencing analysis of three amylase cDNAs in the shrimp Penaeus vannamei (Crustacea decapoda): Evolutionary aspects
    • DOI 10.1007/BF02352284
    • Van Wormhoudt A, Sellos DY. 1996. Cloning and sequencing analysis of three amylase cDNAs in the shrimp Pennaeus vannamei (Crustacae decapoda): evolutionary aspects. Journal of Molecular Evolution 42: 543-551. (Pubitemid 26197144)
    • (1996) Journal of Molecular Evolution , vol.42 , Issue.5 , pp. 543-551
    • Van Wormhoudt, A.1    Sellos, D.2
  • 39
    • 77956724014 scopus 로고
    • The biochemistry of sugars and polysaccharides in insects
    • Wyatt GR. 1967. The biochemistry of sugars and polysaccharides in insects. Advance in Insect Physiology 4: 287-360
    • (1967) Advance in Insect Physiology , vol.4 , pp. 287-360
    • Wyatt, G.R.1
  • 40
    • 0006130893 scopus 로고
    • Japanese society for promotion of science. Ueno Park, Tokyo
    • Yokoyama T. 1959. Silkworm Genetics Illustrated. Japanese society for promotion of science. Ueno Park, Tokyo.
    • (1959) Silkworm Genetics Illustrated
    • Yokoyama, T.1


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