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Volumn 26, Issue 8-9, 1996, Pages 859-865

L-Dopa decarboxylase mRNA levels are correlated with the L-Dopa decarboxylase protein profile during the development of the insect Ceratitis capitata

Author keywords

Ceratitis capitata; DDC activity; Immunoprecipitation; in vitro translation; Insect development; L Dopa decarboxylase

Indexed keywords

AROMATIC LEVO AMINO ACID DECARBOXYLASE; MESSENGER RNA;

EID: 0030240395     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(96)00047-1     Document Type: Article
Times cited : (4)

References (32)
  • 1
    • 0015356037 scopus 로고
    • Purification of biologically active globin messenger RNA by chromatography on oligothyraidylic acid-cellulose
    • Aviv H. and Leder P. (1972) Purification of biologically active globin messenger RNA by chromatography on oligothyraidylic acid-cellulose, Proc. Natl Acad. Sci. U.S.A., 69, 1408-1412.
    • (1972) Proc. Natl Acad. Sci. U.S.A. , vol.69 , pp. 1408-1412
    • Aviv, H.1    Leder, P.2
  • 2
    • 0020352067 scopus 로고
    • The use of Tween-20 as a blocking agent in the immunological detection of proteins transferred to nitrocellulose membranes
    • Batteiger B., Newhall V. W. J. and Jones R. B. (1982) The use of Tween-20 as a blocking agent in the immunological detection of proteins transferred to nitrocellulose membranes. J. Immunol. Meth. 55, 297-307.
    • (1982) J. Immunol. Meth. , vol.55 , pp. 297-307
    • Batteiger, B.1    Newhall, V.W.J.2    Jones, R.B.3
  • 3
    • 0029985534 scopus 로고    scopus 로고
    • Purification and characterization of L-Dopa decarboxylase from pharate pupae of Ceratitis capitata. A comparison with the enzyme purified from the white prepupae
    • Bossinakou K.S. and Fragoulis E.G. (1996) Purification and characterization of L-Dopa decarboxylase from pharate pupae of Ceratitis capitata. A comparison with the enzyme purified from the white prepupae. Comp. Biochem. Physiol. 113, 213-220.
    • (1996) Comp. Biochem. Physiol. , vol.113 , pp. 213-220
    • Bossinakou, K.S.1    Fragoulis, E.G.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram, quantities of protein utilising the principle of protein-dye binding
    • Bradford M.M. (1976) A rapid and sensitive method for the quantitation of microgram, quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0025736627 scopus 로고
    • A two-cycle immunoprecipitation procedure for reducing nonspecific protein contamination
    • Doolittle M.H., Martin D.C., Davis R.C., Reuben M.A. and Elovson J. (1991) A two-cycle immunoprecipitation procedure for reducing nonspecific protein contamination. Analyt Biochem. 195, 364-368.
    • (1991) Analyt Biochem. , vol.195 , pp. 364-368
    • Doolittle, M.H.1    Martin, D.C.2    Davis, R.C.3    Reuben, M.A.4    Elovson, J.5
  • 7
    • 0014945408 scopus 로고
    • Structure and function of mammalian ribosomes-I. Isolation and characterization of active liver ribosome subunits
    • Falvey A.K. and Staehelin T. (1970) Structure and function of mammalian ribosomes-I. Isolation and characterization of active liver ribosome subunits. J. Mol. Biol. 53, 1-19.
    • (1970) J. Mol. Biol. , vol.53 , pp. 1-19
    • Falvey, A.K.1    Staehelin, T.2
  • 8
    • 0016834093 scopus 로고
    • Purification and characteristics of Dopa decarboxylase from the integument of Calliphora vicina larvae
    • Fragoulis E.G. and Sekeris C.E. (1975a) Purification and characteristics of Dopa decarboxylase from the integument of Calliphora vicina larvae. Arch. Biochem. Biophys. 168, 15-25.
    • (1975) Arch. Biochem. Biophys. , vol.168 , pp. 15-25
    • Fragoulis, E.G.1    Sekeris, C.E.2
  • 9
    • 0016436940 scopus 로고
    • Induction of dopa (3,4-dihydroxyphenylalanine) decarboxylase in blowfly integument by ecdysone
    • Fragoulis E.G. and Sekeris C.E. (1975b) Induction of dopa (3,4-dihydroxyphenylalanine) decarboxylase in blowfly integument by ecdysone. Biochem. J. 146, 121-126.
    • (1975) Biochem. J. , vol.146 , pp. 121-126
    • Fragoulis, E.G.1    Sekeris, C.E.2
  • 10
    • 0021921447 scopus 로고
    • An analysis of dopa decarboxylase expression during embryogenesis in Drosophila melanogaster
    • Gietz R.D. and Hodgetts R.B. (1985) An analysis of dopa decarboxylase expression during embryogenesis in Drosophila melanogaster. Dev. Biol. 107, 142-155.
    • (1985) Dev. Biol. , vol.107 , pp. 142-155
    • Gietz, R.D.1    Hodgetts, R.B.2
  • 11
    • 38249043470 scopus 로고
    • Inhibition of dopa decarboxylase synthesis by 20-hydroxyecdysone during the last larval moult of Manduca sexta
    • Minima K. and Riddiford L.M. (1986) Inhibition of dopa decarboxylase synthesis by 20-hydroxyecdysone during the last larval moult of Manduca sexta. Insect Biochem. 16, 225-231.
    • (1986) Insect Biochem. , vol.16 , pp. 225-231
    • Hiruma, K.1    Riddiford, L.M.2
  • 12
    • 0025250083 scopus 로고
    • Regulation of dopa decarboxylase gene expression in the larval epidermis of the tobacco homworm by 20-hydroxyecdysone and juvenile hormone
    • Hiruma K. and Riddiford L.M. (1990) Regulation of dopa decarboxylase gene expression in the larval epidermis of the tobacco homworm by 20-hydroxyecdysone and juvenile hormone. Dev. Biol. 138, 214-224.
    • (1990) Dev. Biol. , vol.138 , pp. 214-224
    • Hiruma, K.1    Riddiford, L.M.2
  • 13
    • 0029047692 scopus 로고
    • Characterization of the dopa decarboxylase gene of Manduca sexta and its suppression by 20-hydroxyecdysone
    • Hiruma K., Carter M.S. and Riddiford L.M. (1995) Characterization of the dopa decarboxylase gene of Manduca sexta and its suppression by 20-hydroxyecdysone. Dev. Biol. 169, 195-209.
    • (1995) Dev. Biol. , vol.169 , pp. 195-209
    • Hiruma, K.1    Carter, M.S.2    Riddiford, L.M.3
  • 14
    • 0011442195 scopus 로고
    • Zum Tyrosinstoffwechsel der Insekten, VI: Identifizierung von N-acetyl-3,4-dihydroxy-β-phenatnylamin (N-acetyl-dopamine) als Tyrosinmetabolit
    • Karlson P., Sekeris C.E. and Sekeri K.E. (1962) Zum Tyrosinstoffwechsel der Insekten, VI: Identifizierung von N-Acetyl-3,4-dihydroxy-β-phenatnylamin (N-acetyl-dopamine) als Tyrosinmetabolit. Hoppe-Seylers Z. Physiol. Chem. 327, 86-94.
    • (1962) Hoppe-Seylers Z. Physiol. Chem. , vol.327 , pp. 86-94
    • Karlson, P.1    Sekeris, C.E.2    Sekeri, K.E.3
  • 15
    • 0001012621 scopus 로고
    • N-acetyl-dopamine as sclerotizing agent of the insect cuticle
    • Karlson P. and Sekeris C.E. (1962) N-acetyl-dopamine as sclerotizing agent of the insect cuticle. Nature 195, 183-184.
    • (1962) Nature , vol.195 , pp. 183-184
    • Karlson, P.1    Sekeris, C.E.2
  • 17
    • 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
  • 18
    • 0020540310 scopus 로고
    • Genetic dissection of monoamine neurotransmitter synthesis in Drosophila
    • Livingstone M. and Tempel B. (1983) Genetic dissection of monoamine neurotransmitter synthesis in Drosophila. Nature 303, 6770-6774.
    • (1983) Nature , vol.303 , pp. 6770-6774
    • Livingstone, M.1    Tempel, B.2
  • 20
    • 0019168655 scopus 로고
    • Developmental relationship between dopa decarboxylase, dopamine acetyl-transferase and ecdysone in Drosophila
    • March S.L. and Wright T.R.F. (1980) Developmental relationship between dopa decarboxylase, dopamine acetyl-transferase and ecdysone in Drosophila. Dev. Biol. 80, 379-387.
    • (1980) Dev. Biol. , vol.80 , pp. 379-387
    • March, S.L.1    Wright, T.R.F.2
  • 21
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin J., Mayhew M., Langer T. and Hartl U. (1993) The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366, 228-233.
    • (1993) Nature , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, U.4
  • 22
    • 0000442130 scopus 로고
    • Purification and characterization of L-dopa decarboxylase from the white puparia of Ceratitis capitata
    • Mappouras D.G. and Fragoulis E.G. (1988) Purification and characterization of L-dopa decarboxylase from the white puparia of Ceratitis capitata. Insect Biochem. 18, 369-376.
    • (1988) Insect Biochem. , vol.18 , pp. 369-376
    • Mappouras, D.G.1    Fragoulis, E.G.2
  • 23
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins
    • Merril C.R., Goldman D., Sedman S.A. and Ebert M.H. (1981) Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins. Science 211, 1437-1438.
    • (1981) Science , vol.211 , pp. 1437-1438
    • Merril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 24
    • 3543052553 scopus 로고
    • Regulated splicing produces different forms of dopa decarboxylase in the central nervous system and hypoderm of Drosophila melanogaster
    • Morgan B.A., Johnson W.A. and Hirsh J. (1986) Regulated splicing produces different forms of dopa decarboxylase in the central nervous system and hypoderm of Drosophila melanogaster. EMBO J. 5, 3335-3342.
    • (1986) EMBO J. , vol.5 , pp. 3335-3342
    • Morgan, B.A.1    Johnson, W.A.2    Hirsh, J.3
  • 25
    • 0002313542 scopus 로고
    • Ecdysone during insect developmental activities in some enzymes of tyrosine metabolism in comparison with ecdysone titer during the development of the blowfly Calliphora erythrocephala
    • Shaaya E. and Sekeris C.E. (1965) Ecdysone during insect developmental activities in some enzymes of tyrosine metabolism in comparison with ecdysone titer during the development of the blowfly Calliphora erythrocephala. Gen. Comp. Endocrinol. 5, 35-39.
    • (1965) Gen. Comp. Endocrinol. , vol.5 , pp. 35-39
    • Shaaya, E.1    Sekeris, C.E.2
  • 26
    • 0015929572 scopus 로고
    • Initiation of mammalian protein synthesis: The importance of ribosome and initiation factor quality for the efficiency of in vitro systems
    • Schreier M. and Staehelin T. (1973) Initiation of mammalian protein synthesis: the importance of ribosome and initiation factor quality for the efficiency of in vitro systems. J. Mol. Biol. 73, 329-349.
    • (1973) J. Mol. Biol. , vol.73 , pp. 329-349
    • Schreier, M.1    Staehelin, T.2
  • 27
    • 0011389465 scopus 로고
    • Zum Tyrosinstoffwechsel der Insekten; VII: Der katabolische Abbau des Tyrosins und die Biogenese der Sklerotisierungssubstanz N-Acetyldopamin
    • Sekeris C.E. and Karlson P. (1962) Zum Tyrosinstoffwechsel der Insekten; VII: Der katabolische Abbau des Tyrosins und die Biogenese der Sklerotisierungssubstanz N-Acetyldopamin. Biochem. Biophys. Acta 62, 103-113.
    • (1962) Biochem. Biophys. Acta , vol.62 , pp. 103-113
    • Sekeris, C.E.1    Karlson, P.2
  • 28
    • 0023654586 scopus 로고
    • Purification and characterization of a ribonuclease specific for poly(U) and poly(C) from the larvae of Ceratitis capitata
    • Sideris D.C. and Fragoulis E.G. (1987) Purification and characterization of a ribonuclease specific for poly(U) and poly(C) from the larvae of Ceratitis capitata. Eur. J. Biochem. 164, 309-315.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 309-315
    • Sideris, D.C.1    Fragoulis, E.G.2
  • 29
    • 0011443302 scopus 로고
    • Properties of a partially purified inhibitor of protein synthesis from the post ribosomal supernatant of six-day-old larvae of Ceratitis capitata
    • Sideris D.C. and Fragoulis E.G. (1989) Properties of a partially purified inhibitor of protein synthesis from the post ribosomal supernatant of six-day-old larvae of Ceratitis capitata. Comp. Biochem. Physiol. 93B, 657-664.
    • (1989) Comp. Biochem. Physiol. , vol.93 B , pp. 657-664
    • Sideris, D.C.1    Fragoulis, E.G.2
  • 30
    • 0019061278 scopus 로고
    • Hybridization of denatured RNA and small DNA fragments tranferred to nitrocellulose
    • Thomas P. S. (1980) Hybridization of denatured RNA and small DNA fragments tranferred to nitrocellulose. Proc. Natl Acad. Sci. U.S.A., 77, 5201-5205.
    • (1980) Proc. Natl Acad. Sci. U.S.A. , vol.77 , pp. 5201-5205
    • Thomas, P.S.1
  • 31
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T. and Gordon J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. U.S.A., 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 32
    • 0001104991 scopus 로고
    • Haemolymph ecdysteroid titres at metamorphosis in the fruit fly Ceratitis capitata: Multiple peaks not apparent in whole body extracts
    • Vafopoulou X., Steel C.G., Aleporou-Marinou V. and Patargias T. (1992) Haemolymph ecdysteroid titres at metamorphosis in the fruit fly Ceratitis capitata: multiple peaks not apparent in whole body extracts. Physiol. Entomol. 17, 380-386.
    • (1992) Physiol. Entomol. , vol.17 , pp. 380-386
    • Vafopoulou, X.1    Steel, C.G.2    Aleporou-Marinou, V.3    Patargias, T.4


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