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Volumn 28, Issue 12, 1998, Pages 995-1005

Purification and properties of two blue biliproteins from the larval hemolymph and integument of Rhodinia fugax (Lepidoptera: Saturniidae)

Author keywords

Biliprotein; Biliverdin binding protein; Hemolymph protein; Insecticyanin; Lepidoptera; Rhodinia fugax; Satumiidae

Indexed keywords

BILIPROTEIN; BINDING PROTEIN; BLUE BILIPROTEIN; INSECT PROTEIN; UNCLASSIFIED DRUG;

EID: 0032407354     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(98)00088-5     Document Type: Article
Times cited : (14)

References (35)
  • 1
    • 0001497528 scopus 로고
    • The status of blue-green bile pigments of butterflies, and their phototransformations
    • Barbier M. The status of blue-green bile pigments of butterflies, and their phototransformations. Experientia. 37:1981;1060-1062.
    • (1981) Experientia , vol.37 , pp. 1060-1062
    • Barbier, M.1
  • 2
    • 0013506364 scopus 로고
    • The pigments of Papilio graphium weiskei: Sarpedobilin and ommin responsible for a unique pattern in a butterfly wing membrane
    • Barbier M. The pigments of Papilio graphium weiskei: sarpedobilin and ommin responsible for a unique pattern in a butterfly wing membrane. Comp. Biochem. Physiol. 76B:1983;57-59.
    • (1983) Comp. Biochem. Physiol. , vol.76 , pp. 57-59
    • Barbier, M.1
  • 3
    • 0013471895 scopus 로고
    • Pterobiline, phorcabiline et sarpedobiline, pigments biliaires IX isoles de Lepidopteres
    • Thesis, Orsay University, 122 pp.
    • Bois-Choussy, M., 1977. Pterobiline, phorcabiline et sarpedobiline, pigments biliaires IX isoles de Lepidopteres. Biosyntheses, reactivite et structures. Thesis, Orsay University, 122 pp.
    • (1977) Biosyntheses, Reactivite et Structures
    • Bois-Choussy, M.1
  • 4
    • 0013507361 scopus 로고
    • Preliminary report on the neopterobilins, blue green pigments from Lepidoptera
    • Choussy M., Barbier M., Rudiger W., Klose W. Preliminary report on the neopterobilins, blue green pigments from Lepidoptera. Comp. Biochem. Physiol. 44B:1973;47-52.
    • (1973) Comp. Biochem. Physiol. , vol.44 , pp. 47-52
    • Choussy, M.1    Barbier, M.2    Rudiger, W.3    Klose, W.4
  • 6
    • 0022432687 scopus 로고
    • Purification and characterization of a biliverdin-associated protein from the hemolymph of Manduca sexta
    • Goodman W.G., Adams B., Trost J.T. Purification and characterization of a biliverdin-associated protein from the hemolymph of Manduca sexta. Biochemistry. 24:1985;1168-1175.
    • (1985) Biochemistry , vol.24 , pp. 1168-1175
    • Goodman, W.G.1    Adams, B.2    Trost, J.T.3
  • 7
    • 0023058752 scopus 로고
    • A larval specific lipoprotein: Purification and characterization of a blue chromoprotein from Heliothis zea
    • Haunerland N.H., Bowers W.S. A larval specific lipoprotein: purification and characterization of a blue chromoprotein from Heliothis zea. Biochem. Biophys. Res. Commun. 134:1986;580-586.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 580-586
    • Haunerland, N.H.1    Bowers, W.S.2
  • 8
    • 0025145811 scopus 로고
    • Microsequencing of proteins electrotransferred onto immobilizing matrices from polyacrylamide gel electrophoresis: Application to an insoluble protein
    • Hirano H., Watanabe T. Microsequencing of proteins electrotransferred onto immobilizing matrices from polyacrylamide gel electrophoresis: application to an insoluble protein. Electrophoresis. 11:1990;573-580.
    • (1990) Electrophoresis , vol.11 , pp. 573-580
    • Hirano, H.1    Watanabe, T.2
  • 9
    • 0023056525 scopus 로고
    • Crystallization of insecticyanin from the hemolymph of the tobacco hornworm Manduca sexta L. in a form suitable for a high resolution structure determination
    • Holden H.M., Law J.H., Rayment I. Crystallization of insecticyanin from the hemolymph of the tobacco hornworm Manduca sexta L. in a form suitable for a high resolution structure determination. J. Biol. Chem. 261:1986;4217-4218.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4217-4218
    • Holden, H.M.1    Law, J.H.2    Rayment, I.3
  • 10
    • 0023352067 scopus 로고
    • The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 Å resolution
    • Holden H.M., Rypniewski W.R., Law J.H., Rayment I. The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 Å resolution. EMBO J. 6:1987;1565-1570.
    • (1987) EMBO J. , vol.6 , pp. 1565-1570
    • Holden, H.M.1    Rypniewski, W.R.2    Law, J.H.3    Rayment, I.4
  • 11
    • 0023660428 scopus 로고
    • Crystallization, crystal structure analysis and preliminary molecular model of bilin binding protein from the insect Pieris brassicae
    • Huber R., Schneider M., Epp O., Mayr I., Messerschmidt A., Pflugrath J., Kayser H. Crystallization, crystal structure analysis and preliminary molecular model of bilin binding protein from the insect Pieris brassicae. J. Mol. Biol. 195:1987;423-434.
    • (1987) J. Mol. Biol. , vol.195 , pp. 423-434
    • Huber, R.1    Schneider, M.2    Epp, O.3    Mayr, I.4    Messerschmidt, A.5    Pflugrath, J.6    Kayser, H.7
  • 12
  • 13
    • 84990420817 scopus 로고
    • Purification and characterization of a very high density chromolipoprotein from the hemolymph of Trichoplusia ni (Hübner)
    • Jones G., Ryan R.O., Haunerland N.H., Law J.H. Purification and characterization of a very high density chromolipoprotein from the hemolymph of Trichoplusia ni (Hübner). Arch. Insect Biochem. Physiol. 7:1988;1-11.
    • (1988) Arch. Insect Biochem. Physiol. , vol.7 , pp. 1-11
    • Jones, G.1    Ryan, R.O.2    Haunerland, N.H.3    Law, J.H.4
  • 14
    • 0002162530 scopus 로고
    • Cocoon coloration and its determination factor in Rhodinia fugax
    • Kato Y., Miyata T. Cocoon coloration and its determination factor in Rhodinia fugax. Int. J. Wild Silkmoth and Silk. 1:1994;53-55.
    • (1994) Int. J. Wild Silkmoth and Silk , vol.1 , pp. 53-55
    • Kato, Y.1    Miyata, T.2
  • 16
  • 17
    • 0021795948 scopus 로고
    • Temporal programming of epidermal cell protein synthesis during the larval-pupal transformation of Manduca sexta
    • Kiely M.L., Riddiford L.M. Temporal programming of epidermal cell protein synthesis during the larval-pupal transformation of Manduca sexta. Roux's Arch. Dev. Biol. 194:1985;325-335.
    • (1985) Roux's Arch. Dev. Biol. , vol.194 , pp. 325-335
    • Kiely, M.L.1    Riddiford, L.M.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0024962459 scopus 로고
    • Insects as biochemical models
    • Law J.H., Wells M.A. Insects as biochemical models. J. Biol. Chem. 264:1989;16335-16338.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16335-16338
    • Law, J.H.1    Wells, M.A.2
  • 20
    • 0026605063 scopus 로고
    • Two distinct genes encode two major isoelectric forms of insecticyanin in the tobacco hornworm, Manduca sexta
    • Li W.-C., Riddiford L.M. Two distinct genes encode two major isoelectric forms of insecticyanin in the tobacco hornworm, Manduca sexta. Eur. J. Biochem. 205:1992;491-499.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 491-499
    • Li, W.-C.1    Riddiford, L.M.2
  • 21
    • 0023053570 scopus 로고
    • Preliminary characterization of crystals of the protein insecticyanin from the tobacco hornworm Manduca sexta L.
    • Petratos K., Tsernoglou D., Cherbas P. Preliminary characterization of crystals of the protein insecticyanin from the tobacco hornworm Manduca sexta L. J. Mol. Biol. 189:1986;727.
    • (1986) J. Mol. Biol. , vol.189 , pp. 727
    • Petratos, K.1    Tsernoglou, D.2    Cherbas, P.3
  • 22
    • 0020170076 scopus 로고
    • Changes in translatable mRNAs during the larval-pupal transformation of epidermis of the tobacco hornworm
    • Riddiford L.M. Changes in translatable mRNAs during the larval-pupal transformation of epidermis of the tobacco hornworm. Dev. Biol. 92:1982;330-342.
    • (1982) Dev. Biol. , vol.92 , pp. 330-342
    • Riddiford, L.M.1
  • 24
    • 0021686359 scopus 로고
    • The covalent protein structure of insecticyanin, a blue biliprotein from the hemolymph of the tobacco hornworm, Manduca sexta L.
    • Riley C.T., Barbeau B.K., Keim P.S., Kezdy F.J., Heinrikson R.L., Law J.H. The covalent protein structure of insecticyanin, a blue biliprotein from the hemolymph of the tobacco hornworm, Manduca sexta L. J. Biol. Chem. 259:1984;13159-13165.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13159-13165
    • Riley, C.T.1    Barbeau, B.K.2    Keim, P.S.3    Kezdy, F.J.4    Heinrikson, R.L.5    Law, J.H.6
  • 25
    • 0027191368 scopus 로고
    • Purification and characterization of a biliverdin-binding protein from the molting fluid of the eri silkworm, Samia cynthia ricini
    • Saito H. Purification and characterization of a biliverdin-binding protein from the molting fluid of the eri silkworm, Samia cynthia ricini. Comp. Biochem. Physiol. 105B:1993;473-479.
    • (1993) Comp. Biochem. Physiol. , vol.105 , pp. 473-479
    • Saito, H.1
  • 26
    • 0000040648 scopus 로고
    • N-terminal amino acid sequence of the biliverdin-binding protein (BBP) from the molting fluid of the eri silkworm, Samia cynthia ricini
    • Saito H. N-terminal amino acid sequence of the biliverdin-binding protein (BBP) from the molting fluid of the eri silkworm, Samia cynthia ricini. Int. J. Wild Silkmoth and Silk. 1:1994;213-217.
    • (1994) Int. J. Wild Silkmoth and Silk , vol.1 , pp. 213-217
    • Saito, H.1
  • 27
    • 0001180774 scopus 로고    scopus 로고
    • Purification and characterization of a biliverdin-binding protein from the larval cuticle of the saturniid silkworm, Attacus atlas
    • Saito H. Purification and characterization of a biliverdin-binding protein from the larval cuticle of the saturniid silkworm, Attacus atlas. Int. J. Wild Silkmoth and Silk. 3:1997;1-6.
    • (1997) Int. J. Wild Silkmoth and Silk , vol.3 , pp. 1-6
    • Saito, H.1
  • 28
    • 0032510283 scopus 로고    scopus 로고
    • Purification and characterization of two insecticyanin-type proteins from the larval hemolymph of the Eri-silkworm, Samia cynthia ricini
    • Saito H. Purification and characterization of two insecticyanin-type proteins from the larval hemolymph of the Eri-silkworm, Samia cynthia ricini. Biochim. Biophys. Acta. 1380:1998;141-150.
    • (1998) Biochim. Biophys. Acta , vol.1380 , pp. 141-150
    • Saito, H.1
  • 29
    • 0031240828 scopus 로고    scopus 로고
    • Insecticyanin of Agrius convolvuli: Purification and characterization of the biliverdin-binding protein from the larval hemolymph
    • Saito H., Shimoda M. Insecticyanin of Agrius convolvuli: purification and characterization of the biliverdin-binding protein from the larval hemolymph. Zool. Sci. 14:1997;777-783.
    • (1997) Zool. Sci. , vol.14 , pp. 777-783
    • Saito, H.1    Shimoda, M.2
  • 30
    • 0031815317 scopus 로고    scopus 로고
    • Isolation and partial characterization of the chromoprotein from the larval hemolymph of the Japanese oak silkworm Antheraea yamamai
    • Saito H., Yamada H., Kato Y. Isolation and partial characterization of the chromoprotein from the larval hemolymph of the Japanese oak silkworm Antheraea yamamai. Comp. Biochem. Physiol. 119B:1998;625-630.
    • (1998) Comp. Biochem. Physiol. , vol.119 , pp. 625-630
    • Saito, H.1    Yamada, H.2    Kato, Y.3
  • 31
    • 0024030725 scopus 로고
    • The complete amino-acid sequence of the bilin-binding protein from Pieris brassicae and its similarity to a family of serum transport proteins like the retinol-binding proteins
    • Suter F., Kayser H., Zuber H. The complete amino-acid sequence of the bilin-binding protein from Pieris brassicae and its similarity to a family of serum transport proteins like the retinol-binding proteins. Biol. Chem. Hoppe-Seyler. 369:1988;497-505.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 497-505
    • Suter, F.1    Kayser, H.2    Zuber, H.3
  • 33
    • 0002861784 scopus 로고
    • Purification and properties of a blue chromoprotein in the hemolymph of the Japanese oak silkworm Antheraea yamamai
    • In: Akai, H., Wu, Z.S. (Eds.), International Society for Wild Silkmoths
    • Yamada, H., Kato, Y., 1989. Purification and properties of a blue chromoprotein in the hemolymph of the Japanese oak silkworm Antheraea yamamai. In: Akai, H., Wu, Z.S. (Eds.), Wild Silkmoths '88. International Society for Wild Silkmoths, pp. 41-48.
    • (1989) Wild Silkmoths '88 , pp. 41-48
    • Yamada, H.1    Kato, Y.2
  • 34
    • 0001834286 scopus 로고
    • Characteristic properties of a blue chromoprotein in larval hemolymph of Antheraea yamamai
    • In: Akai, H., Kiuchi, M. (Eds.), International Society for Wild Silkmoths
    • Yamada, H., Kato, Y., 1991. Characteristic properties of a blue chromoprotein in larval hemolymph of Antheraea yamamai. In: Akai, H., Kiuchi, M. (Eds.), Wild Silkmoths '89-'90. International Society for Wild Silkmoths, pp. 89-95.
    • (1991) Wild Silkmoths '89-'90 , pp. 89-95
    • Yamada, H.1    Kato, Y.2
  • 35
    • 0029103784 scopus 로고
    • Purification and characterization of four biliverdin-binding proteins from larval hemolymph of the common cutworm, Spodoptera litura
    • Yoshiga T., Tojo S. Purification and characterization of four biliverdin-binding proteins from larval hemolymph of the common cutworm, Spodoptera litura. Insect Biochem. Mol. Biol. 25:1995;575-581.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 575-581
    • Yoshiga, T.1    Tojo, S.2


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