메뉴 건너뛰기




Volumn 13, Issue 3, 2003, Pages 147-157

Structural determination of the N-glycans of a lepidopteran arylphorin reveals the presence of a monoglucosylated oligosaccharide in the storage protein

Author keywords

Antheraea pernyi storage protein; Arylphorin; Glycosylation; Monoglucosylated oligomannose

Indexed keywords

ALPHA MANNOSIDASE; ARYLPHORIN; CARBOHYDRATE; GLYCAN DERIVATIVE; GLYCOPROTEIN; INSECT PROTEIN; MANNOSE; OLIGOSACCHARIDE; STORAGE PROTEIN; UNCLASSIFIED DRUG;

EID: 0037366674     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwg023     Document Type: Article
Times cited : (36)

References (45)
  • 1
    • 0033902975 scopus 로고    scopus 로고
    • N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: Effects of mammalian galactosyltransferase
    • Ailor, E., Takahashi, N., Tsukamoto, Y., Masuda, K., Rahman, B.A., Jarvis, D.L., Lee, Y.C., and Betenbaugh, M.J. (2000) N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: effects of mammalian galactosyltransferase. Glycobiology, 10, 837-847.
    • (2000) Glycobiology , vol.10 , pp. 837-847
    • Ailor, E.1    Takahashi, N.2    Tsukamoto, Y.3    Masuda, K.4    Rahman, B.A.5    Jarvis, D.L.6    Lee, Y.C.7    Betenbaugh, M.J.8
  • 2
    • 0027772780 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells
    • Altmann, F., Kornfeld, G., Dalik, T., Staudacher, E., and Glossl, J. (1993) Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells. Glycobiology, 3, 619-625.
    • (1993) Glycobiology , vol.3 , pp. 619-625
    • Altmann, F.1    Kornfeld, G.2    Dalik, T.3    Staudacher, E.4    Glossl, J.5
  • 3
    • 0030136308 scopus 로고    scopus 로고
    • Purification and characterization of two storage proteins from Locusta migratoria showing distinct developmental and hormonal regulation
    • Ancsin, J.B. and Wyatt, G.B. (1996) Purification and characterization of two storage proteins from Locusta migratoria showing distinct developmental and hormonal regulation. Insect Biochem. Mol. Biol., 26, 501-510.
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 501-510
    • Ancsin, J.B.1    Wyatt, G.B.2
  • 5
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge, J.C., Patel, T.P., Bruce, J.A., Goulding, P.N., Charles, S.M., and Parekh, R.B. (1995) Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem., 230, 229-238.
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 6
    • 0035933794 scopus 로고    scopus 로고
    • Monoglucosylated oligomannosides are released during the degradation process of newly synthesized glycoproteins
    • Cacan, R., Duvet, S., Labiau, O., Verbert, A., and Krag. S.S. (2001) Monoglucosylated oligomannosides are released during the degradation process of newly synthesized glycoproteins. J. Biol. Chem., 276, 22307-22312.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22307-22312
    • Cacan, R.1    Duvet, S.2    Labiau, O.3    Verbert, A.4    Krag, S.S.5
  • 7
    • 0025336176 scopus 로고
    • Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells
    • Davidson, D.J., Fraser, M.J., and Castellino, F.J. (1990) Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells. Biochemistry, 29, 5584-5590.
    • (1990) Biochemistry , vol.29 , pp. 5584-5590
    • Davidson, D.J.1    Fraser, M.J.2    Castellino, F.J.3
  • 8
    • 0023642618 scopus 로고
    • Characterization of N-linked gluco-oligomannose type of carbohydrate chains of glycoproteins from the ovary of the starfish Asterias rubens (L.)
    • De Waard, P., Kamerling, J.P., Van Halbeek, H., Vliegenthart, J.F., and Broertjes, J.J. (1987) Characterization of N-linked gluco-oligomannose type of carbohydrate chains of glycoproteins from the ovary of the starfish Asterias rubens (L.). Eur. J. Biochem., 168, 679-685.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 679-685
    • De Waard, P.1    Kamerling, J.P.2    Van Halbeek, H.3    Vliegenthart, J.F.4    Broertjes, J.J.5
  • 9
    • 0023131286 scopus 로고
    • Structures of the sugar chains of a major glycoprotein present in the egg jelly coat of a starfish, Asterias amurensis
    • Endo, T., Hoshi, M., Endo, S., Arata, Y., and Kobata, A. (1987) Structures of the sugar chains of a major glycoprotein present in the egg jelly coat of a starfish, Asterias amurensis. Arch. Biochem. Biophys., 252, 105-112.
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 105-112
    • Endo, T.1    Hoshi, M.2    Endo, S.3    Arata, Y.4    Kobata, A.5
  • 10
    • 0024962158 scopus 로고
    • Structure of the gene for the arylphorin-type storage protein SP 2 of Bombyx mori
    • Fujii, T., Sakurai, H., Izumi, S., and Tomino, S. (1989) Structure of the gene for the arylphorin-type storage protein SP 2 of Bombyx mori. J. Biol. Chem., 264, 11020-11025.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11020-11025
    • Fujii, T.1    Sakurai, H.2    Izumi, S.3    Tomino, S.4
  • 11
    • 0031048315 scopus 로고    scopus 로고
    • A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces
    • Funk, V.A., Thomas-Oates, J.E., Kielland, S.L., Bates, P.A., and Olafson, R.W. (1997) A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces. Mol. Biochem. Parasitol., 84, 33-48.
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 33-48
    • Funk, V.A.1    Thomas-Oates, J.E.2    Kielland, S.L.3    Bates, P.A.4    Olafson, R.W.5
  • 12
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • Guile, G.R., Rudd, P.M., Wing, D.R., and Dwek, R.A. (1996) A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal. Biochem., 240, 210-226.
    • (1996) Anal. Biochem. , vol.240 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Dwek, R.A.4
  • 13
    • 0027405920 scopus 로고
    • Structure of the asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein
    • Hard, K., Van Doorn, J.M., Thomas-Oates, J.E., Kamerling, J.P., and Van der Horst, D.J. (1993) Structure of the asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein. Biochemistry, 32, 766-775.
    • (1993) Biochemistry , vol.32 , pp. 766-775
    • Hard, K.1    Van Doorn, J.M.2    Thomas-Oates, J.E.3    Kamerling, J.P.4    Van der Horst, D.J.5
  • 14
    • 0030240428 scopus 로고    scopus 로고
    • Insect storage proteins: Gene families and receptors
    • Haunerland, N.H. (1996) Insect storage proteins: gene families and receptors. Insect Biochem. Mol. Biol., 26, 755-765.
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 755-765
    • Haunerland, N.H.1
  • 15
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius, A. (1994) How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol, Biol. Cell., 5, 253-265.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 16
    • 0021770329 scopus 로고
    • Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells
    • Hsieh, P. and Robbins, P.W. (1984) Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells. J. Biol. Chem., 259, 2375-2382.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2375-2382
    • Hsieh, P.1    Robbins, P.W.2
  • 17
    • 0034031180 scopus 로고    scopus 로고
    • N-glycan processing by a lepidopteran insect α1,2-mannosidase
    • Kawar, Z., Romero, P.A., Herscovics, A., and Jarvis, D.L. (2000) N-glycan processing by a lepidopteran insect α1,2-mannosidase. Glycobiology, 10, 347-355.
    • (2000) Glycobiology , vol.10 , pp. 347-355
    • Kawar, Z.1    Romero, P.A.2    Herscovics, A.3    Jarvis, D.L.4
  • 18
    • 0035844284 scopus 로고    scopus 로고
    • Insect cells encode a class II α-mannosidase with unique properties
    • Kawar, Z., Karaveg, K., Moremen, K.W., and Jarvis, D.L. (2001) Insect cells encode a class II α-mannosidase with unique properties. J. Biol. Chem., 276, 16335-16340.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16335-16340
    • Kawar, Z.1    Karaveg, K.2    Moremen, K.W.3    Jarvis, D.L.4
  • 19
    • 0033567233 scopus 로고    scopus 로고
    • The N-glycans of jack bean α-mannosidase. Structure, topology and function
    • Kimura, Y., Hess, D., and Sturm, A. (1999) The N-glycans of jack bean α-mannosidase. Structure, topology and function. Eur. J. Biochem., 264, 168-175.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 168-175
    • Kimura, Y.1    Hess, D.2    Sturm, A.3
  • 21
    • 0028915061 scopus 로고
    • The asparagine-linked carbohydrate of honeybee venom hyaluronidase
    • Kubelka, V., Altmann, F., and März, L. (1995) The asparagine-linked carbohydrate of honeybee venom hyaluronidase. Glycoconj. J., 12, 77-83.
    • (1995) Glycoconj. J. , vol.12 , pp. 77-83
    • Kubelka, V.1    Altmann, F.2    März, L.3
  • 22
    • 0031571138 scopus 로고    scopus 로고
    • Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography
    • Küster, B., Wheeler, S.F., Hunter, A.P., Dwek, R.A., and Harvey, D.J. (1997) Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography. Anal. Biochem., 250, 82-101.
    • (1997) Anal. Biochem. , vol.250 , pp. 82-101
    • Küster, B.1    Wheeler, S.F.2    Hunter, A.P.3    Dwek, R.A.4    Harvey, D.J.5
  • 23
    • 0032796489 scopus 로고    scopus 로고
    • Use of inhibitors to characterize intermediates in the processing of N-glycans synthesized by insect cells: A metabolic study with Sf9 cell line
    • Marchal, I., Mir, A.M., Kmiecik, D., Verbert, A., and Cacan, R. (1999) Use of inhibitors to characterize intermediates in the processing of N-glycans synthesized by insect cells: a metabolic study with Sf9 cell line. Glycobiology, 9, 645-654.
    • (1999) Glycobiology , vol.9 , pp. 645-654
    • Marchal, I.1    Mir, A.M.2    Kmiecik, D.3    Verbert, A.4    Cacan, R.5
  • 25
    • 77956850407 scopus 로고
    • Protein glycosylation in insects
    • Montreuil, J. and others (eds.), Elsevier, Amsterdam
    • März, L., Altmann, F., Staudacher, E., and Kubelka, V. (1995) Protein glycosylation in insects. In Montreuil, J. and others (eds.), Glycoproteins. Elsevier, Amsterdam, pp. 543-563.
    • (1995) Glycoproteins , pp. 543-563
    • März, L.1    Altmann, F.2    Staudacher, E.3    Kubelka, V.4
  • 26
    • 0027254275 scopus 로고
    • Structures of asparagine linked oligosaccharides of immunoglobulins (IgY) isolated from egg-yolk of Japanese quail
    • Matsuura, F., Ohta, M., Murakami, K., and Matsuki, Y. (1993) Structures of asparagine linked oligosaccharides of immunoglobulins (IgY) isolated from egg-yolk of Japanese quail. Glycoconj. J., 10, 202-213.
    • (1993) Glycoconj. J. , vol.10 , pp. 202-213
    • Matsuura, F.1    Ohta, M.2    Murakami, K.3    Matsuki, Y.4
  • 27
    • 0026329037 scopus 로고
    • Structures of asparagine-linked oligosaccharides from hen egg-yolk antibody (IgY). Occurrence of unusual glucosylated oligo-mannose type oligosaccharides in a mature glycoprotein
    • Ohta, M., Hamako, J., Yamamoto, S., Hatta, H., Kim, M., Yamamoto, T., Oka, S., Mizuochi, T., and Matsuura, F. (1991) Structures of asparagine-linked oligosaccharides from hen egg-yolk antibody (IgY). Occurrence of unusual glucosylated oligo-mannose type oligosaccharides in a mature glycoprotein. Glycoconj. J., 8, 400-413.
    • (1991) Glycoconj. J. , vol.8 , pp. 400-413
    • Ohta, M.1    Hamako, J.2    Yamamoto, S.3    Hatta, H.4    Kim, M.5    Yamamoto, T.6    Oka, S.7    Mizuochi, T.8    Matsuura, F.9
  • 28
    • 0025835386 scopus 로고
    • Detection of the lipid-linked precursor oligosaccharide of N-linked protein glycosylation in Drosophila melanogaster
    • Parker, G.F., Williams, P.J., Butters, T.D., and Roberts, D.B. (1991) Detection of the lipid-linked precursor oligosaccharide of N-linked protein glycosylation in Drosophila melanogaster. FEBS Lett., 290, 58-60.
    • (1991) FEBS Lett. , vol.290 , pp. 58-60
    • Parker, G.F.1    Williams, P.J.2    Butters, T.D.3    Roberts, D.B.4
  • 29
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi, A.J. (2000) Protein glucosylation and its role in protein folding. Annu. Rev. Biochem., 69, 69-93.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 30
    • 0034701053 scopus 로고    scopus 로고
    • Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells
    • Rudd, P.M., Downing, A.K., Cadene, M., Harvey, D.J., Wormald, M.R., Weir, I., Dwek, R.A., Rifkin, D.B., and Gleizes, P.E. (2000) Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells. Biochemistry, 39, 1596-1603.
    • (2000) Biochemistry , vol.39 , pp. 1596-1603
    • Rudd, P.M.1    Downing, A.K.2    Cadene, M.3    Harvey, D.J.4    Wormald, M.R.5    Weir, I.6    Dwek, R.A.7    Rifkin, D.B.8    Gleizes, P.E.9
  • 31
    • 0022426902 scopus 로고
    • Arylphorin from Manduca sexta: Carbohydrate structure and immunological studies
    • Ryan, R.O., Anderson, D.R., Grimes, W.J., and Law, J.H. (1985) Arylphorin from Manduca sexta: carbohydrate structure and immunological studies. Arch. Biochem. Biophys., 243, 115-124.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 115-124
    • Ryan, R.O.1    Anderson, D.R.2    Grimes, W.J.3    Law, J.H.4
  • 32
    • 0023656682 scopus 로고
    • Glycoprotein synthesis in Drosophila Kc cells. Biosynthesis of dolichol-linked saccharides
    • Sagami, H. and Lennarz, W.J. (1987) Glycoprotein synthesis in Drosophila Kc cells. Biosynthesis of dolichol-linked saccharides. J. Biol. Chem., 262, 15610-15617.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15610-15617
    • Sagami, H.1    Lennarz, W.J.2
  • 33
    • 0035086301 scopus 로고    scopus 로고
    • Cloning and expression of Drosophila melanogaster UDP-GlcNAc:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I
    • Sarkar, M. and Schachter, H. (2001) Cloning and expression of Drosophila melanogaster UDP-GlcNAc:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I. Biol. Chem., 382, 209-217.
    • (2001) Biol. Chem. , vol.382 , pp. 209-217
    • Sarkar, M.1    Schachter, H.2
  • 34
    • 85007677752 scopus 로고
    • Characterization of arylphorin of the Eri-silkmoth, Samiacynthia ricini (Donovan) (Lepidoptera: Saturniidae)
    • Shimada, T., Nagata, M., and Yoshitake, N. (1987) Characterization of arylphorin of the Eri-silkmoth, Samiacynthia ricini (Donovan) (Lepidoptera: Saturniidae). Appl. Ent. Zool., 22, 543-552.
    • (1987) Appl. Ent. Zool. , vol.22 , pp. 543-552
    • Shimada, T.1    Nagata, M.2    Yoshitake, N.3
  • 35
    • 0025799819 scopus 로고
    • GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1-6GlcNAc)-Asn-peptide)α1-3-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine
    • Staudacher, E., Altmann, F., Glossl, J., März, L., Schachter, H., Kamerling, J.P., Hard, K., and Vliegenthart, J.F. (1991) GDP-fucose:β-N-acetylglucosamine (Fuc to (Fucα1-6GlcNAc)-Asn-peptide)α1-3-fucosyltransferase activity in honeybee (Apis mellifica) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine. Eur. J. Biochem., 199, 745-751.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 745-751
    • Staudacher, E.1    Altmann, F.2    Glossl, J.3    März, L.4    Schachter, H.5    Kamerling, J.P.6    Hard, K.7    Vliegenthart, J.F.8
  • 36
    • 0024778571 scopus 로고
    • Enzymatic approaches for studying the structure, synthesis, and processing of glycoproteins
    • Tarentino, A.L., Trimble, R.B., and Plummer, T.H. Jr. (1989) Enzymatic approaches for studying the structure, synthesis, and processing of glycoproteins. Methods Cell Biol., 32, 111-139.
    • (1989) Methods Cell Biol. , vol.32 , pp. 111-139
    • Tarentino, A.L.1    Trimble, R.B.2    Plummer T.H., Jr.3
  • 37
    • 0026054117 scopus 로고
    • The function and evolution of insect storage hexamers
    • Telfer, W.H. and Kunkel, J.G. (1991) The function and evolution of insect storage hexamers. Annu. Rev. Entomol., 36, 205-228.
    • (1991) Annu. Rev. Entomol. , vol.36 , pp. 205-228
    • Telfer, W.H.1    Kunkel, J.G.2
  • 38
    • 0001461651 scopus 로고
    • Arylphorin, a new protein from Hyalophora cecropia: Comparisons with calliphorin and manducin
    • Telfer, W.H., Keim, P.S., and Law, J.H. (1983) Arylphorin, a new protein from Hyalophora cecropia: comparisons with calliphorin and manducin. Insect Biochem., 13, 601-613.
    • (1983) Insect Biochem. , vol.13 , pp. 601-613
    • Telfer, W.H.1    Keim, P.S.2    Law, J.H.3
  • 39
    • 0028035562 scopus 로고
    • Purification and characterization of three storage proteins in the common cutworm, Spodoptera litura
    • Tojo, S. and Yoshiga, T. (1993) Purification and characterization of three storage proteins in the common cutworm, Spodoptera litura. Insect Biochem. Mol. Biol., 23, 729-738.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 729-738
    • Tojo, S.1    Yoshiga, T.2
  • 40
    • 0029877528 scopus 로고    scopus 로고
    • Glycosylation in lepidopteran insect cells: Identification of a β1-4-N-acetylgalactosaminyltransferase involved in the synthesis of complex-type oligosaccharide chains
    • Van Die, I., van Tetering, A., Bakker, H., van den Eijnden, D.H., and Joziasse, D.H. (1996) Glycosylation in lepidopteran insect cells: identification of a β1-4-N-acetylgalactosaminyltransferase involved in the synthesis of complex-type oligosaccharide chains. Glycobiology, 6, 157-164.
    • (1996) Glycobiology , vol.6 , pp. 157-164
    • Van Die, I.1    van Tetering, A.2    Bakker, H.3    van den Eijnden, D.H.4    Joziasse, D.H.5
  • 41
    • 0027282196 scopus 로고
    • The presence of UDP-N-acetylglucosamine:α-3-D-mannoside β 1,2-N-acetylglucosaminyltransferase I activity in Spodoptera frugiperda cells (IPLB-SF-21AE) and its enhancement as a result of baculovirus infection
    • Velardo, M.A., Bretthauer, R.K., Boutaud, A., Reinhold, B., Reinhold, V.N., and Castellino, F.J. (1993) The presence of UDP-N-acetylglucosamine:α-3-D-mannoside β 1,2-N-acetylglucosaminyltransferase I activity in Spodoptera frugiperda cells (IPLB-SF-21AE) and its enhancement as a result of baculovirus infection. J. Biol Chem., 268, 17902-17907.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17902-17907
    • Velardo, M.A.1    Bretthauer, R.K.2    Boutaud, A.3    Reinhold, B.4    Reinhold, V.N.5    Castellino, F.J.6
  • 42
    • 0034651589 scopus 로고    scopus 로고
    • Selective organic precipitation/extraction of released N-glycans following large-scale enzymatic deglycosylation of glycoproteins
    • Verostek, M.F., Lubowski, C., and Trimble, R.B. (2000) Selective organic precipitation/extraction of released N-glycans following large-scale enzymatic deglycosylation of glycoproteins. Anal. Biochem., 278, 111-122.
    • (2000) Anal. Biochem. , vol.278 , pp. 111-122
    • Verostek, M.F.1    Lubowski, C.2    Trimble, R.B.3
  • 44
    • 0029893939 scopus 로고    scopus 로고
    • Sequencing analysis of cDNA clones encoding the American cockroach Cr-PI allergens. Homology with insect hemolymph proteins
    • Wu, C.H., Lee, M.F., Liao, S.C., and Luo, S.F. (1996) Sequencing analysis of cDNA clones encoding the American cockroach Cr-PI allergens. Homology with insect hemolymph proteins. J. Biol. Chem., 271, 17937-17943.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17937-17943
    • Wu, C.H.1    Lee, M.F.2    Liao, S.C.3    Luo, S.F.4
  • 45
    • 0034134497 scopus 로고    scopus 로고
    • cDNA cloning and deduced amino acid sequences of three storage proteins in the common cutworm, Spodoptera litura
    • Zheng, Y., Yoshiga, T., and Tojo, S. (2000) cDNA cloning and deduced amino acid sequences of three storage proteins in the common cutworm, Spodoptera litura. Appl. Entomol. Zool., 35, 31-39.
    • (2000) Appl. Entomol. Zool. , vol.35 , pp. 31-39
    • Zheng, Y.1    Yoshiga, T.2    Tojo, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.