메뉴 건너뛰기




Volumn 93, Issue 375, 1998, Pages 85-104

Complex chitinolytic system of Aspergillus fumigatus

Author keywords

Aspergillus fumigatus; Extracellular and cellular enzymes; Multiple chitinases

Indexed keywords

ASPERGILLUS FUMIGATUS;

EID: 0031616363     PISSN: 00262633     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (19)

References (46)
  • 1
    • 0001992646 scopus 로고
    • Regulation of chitin synthase and chitinase in fungi
    • Edited by R. A. A. Muzzarelli. European Chitin Society, Ancona, Italy
    • ADAMS D. J., Causier B. E., Mellor K. J., Keer V., Milling W. and Dada J. 1993. Regulation of chitin synthase and chitinase in fungi. In Chitin Enzymology. pp 15-25. Edited by R. A. A. Muzzarelli. European Chitin Society, Ancona, Italy.
    • (1993) Chitin Enzymology , pp. 15-25
    • Adams, D.J.1    Causier, B.E.2    Mellor, K.J.3    Keer, V.4    Milling, W.5    Dada, J.6
  • 2
    • 0014688461 scopus 로고
    • Biochemical and immunological studies on Aspergillus. II. Immunological properties of protein and polysaccharide fractions from Aspergillus fumigatus
    • AZUMA I., Kimura H., Hirao F., Tsubaru E. and Yamamura Y. 1969. Biochemical and immunological studies on Aspergillus. II. Immunological properties of protein and polysaccharide fractions from Aspergillus fumigatus. Mycopathol. Mycol. Appl. 37 289-303.
    • (1969) Mycopathol. Mycol. Appl. , vol.37 , pp. 289-303
    • Azuma, I.1    Kimura, H.2    Hirao, F.3    Tsubaru, E.4    Yamamura, Y.5
  • 3
    • 0023210141 scopus 로고
    • The synthesis and degradation of chitin
    • CABIB E. 1987. The synthesis and degradation of chitin. Adv. Enzymol. 59 59-101.
    • (1987) Adv. Enzymol. , vol.59 , pp. 59-101
    • Cabib, E.1
  • 4
    • 3643085094 scopus 로고
    • Les mécanismes de la glycosylation et leur importance dans le transport intracellulaire et la secretion des glycoproteines des levures
    • CAILLIEZ J. C. and Poulain D. 1992. Les mécanismes de la glycosylation et leur importance dans le transport intracellulaire et la secretion des glycoproteines des levures. J. Mycol. Med. 2 202-9.
    • (1992) J. Mycol. Med. , vol.2 , pp. 202-209
    • Cailliez, J.C.1    Poulain, D.2
  • 5
    • 0020054384 scopus 로고
    • Endochitinase, a mannan-associated enzyme from Saccharomyces cerevislae
    • CORREA J. V., Elango N., Polacheck I. and Cabib E. 1982. Endochitinase, a mannan-associated enzyme from Saccharomyces cerevislae. J. biol. Chem. 257 1392-7.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1392-1397
    • Correa, J.V.1    Elango, N.2    Polacheck, I.3    Cabib, E.4
  • 6
    • 0016368682 scopus 로고
    • Solubilization and polyacrylamide gel electrophoresis of membrane enzymes with detergents
    • DEWALD B., Dulaney J. T. and Touster O. 1974. Solubilization and polyacrylamide gel electrophoresis of membrane enzymes with detergents. Methods Enzymol. 32 82-91.
    • (1974) Methods Enzymol. , vol.32 , pp. 82-91
    • Dewald, B.1    Dulaney, J.T.2    Touster, O.3
  • 7
    • 0024345556 scopus 로고
    • Chitinase activity from Candida albicans and its inhibition by allosamidin
    • DICKINSON K., Keer V., Hitchcock C. A. and Adams D. J. 1989. Chitinase activity from Candida albicans and its inhibition by allosamidin. J. gen. Microbiol. 135 1417-21.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1417-1421
    • Dickinson, K.1    Keer, V.2    Hitchcock, C.A.3    Adams, D.J.4
  • 8
    • 0015392557 scopus 로고
    • Valeur de l'immunoprécipitation et de l'immunofluoresence indirecte dans les aspergilloses broncho-pulmonaires
    • DROUHET E., Camay L. and Segretain G. 1972. Valeur de l'immunoprécipitation et de l'immunofluoresence indirecte dans les aspergilloses broncho-pulmonaires. Ann. Inst. Pasteur 123 379-95.
    • (1972) Ann. Inst. Pasteur , vol.123 , pp. 379-395
    • Drouhet, E.1    Camay, L.2    Segretain, G.3
  • 10
    • 0028822746 scopus 로고
    • Chitinase activity in human serum and leukocytes
    • ESCOTT G. M. and Adams D. J. 1995. Chitinase activity in human serum and leukocytes. Infect. Immun. 63 4770-3.
    • (1995) Infect. Immun. , vol.63 , pp. 4770-4773
    • Escott, G.M.1    Adams, D.J.2
  • 11
    • 0021360874 scopus 로고
    • Genes required for completion of import proteins into the endoplasmic reticulum in yeast
    • FERRO-NOVICK S., Hansen W., Schauer I. and Scheckman R. 1984. Genes required for completion of import proteins into the endoplasmic reticulum in yeast. J. cell Biol. 98 44-53.
    • (1984) J. Cell Biol. , vol.98 , pp. 44-53
    • Ferro-Novick, S.1    Hansen, W.2    Schauer, I.3    Scheckman, R.4
  • 12
    • 0002928992 scopus 로고
    • Roles of chitinases in fungal growth
    • Edited by R. A. A. Muzzarelli, C. Jeuniaux and G. W. Gooday. Plenum Press, New York
    • GOODAY G. W., Humphries A. M. and McIntosh W. H. 1986. Roles of chitinases in fungal growth. In Chitin in Nature and Technology, pp 83-91. Edited by R. A. A. Muzzarelli, C. Jeuniaux and G. W. Gooday. Plenum Press, New York.
    • (1986) Chitin in Nature and Technology , pp. 83-91
    • Gooday, G.W.1    Humphries, A.M.2    McIntosh, W.H.3
  • 14
    • 0025804919 scopus 로고
    • Immunolocalization of Aspergillus fumigatus mycelial antigens
    • HEARN V. M., Latge J. P. and Prevost M. C. 1991. Immunolocalization of Aspergillus fumigatus mycelial antigens. J. Med. Vet. Mycol. 29 73-81.
    • (1991) J. Med. Vet. Mycol. , vol.29 , pp. 73-81
    • Hearn, V.M.1    Latge, J.P.2    Prevost, M.C.3
  • 15
    • 0028296969 scopus 로고
    • Chemical and immunological analysis of the Aspergillus fumigatus cell wall
    • HEARN V. M. and Sietsma H. 1994. Chemical and immunological analysis of the Aspergillus fumigatus cell wall. Microbiol. 140 789-95.
    • (1994) Microbiol. , vol.140 , pp. 789-795
    • Hearn, V.M.1    Sietsma, H.2
  • 16
    • 0006896289 scopus 로고    scopus 로고
    • Chitinases of the cell surface and wall of Aspergillus fumigatus
    • Edited by R. A. A. Muzzarelli. European Chitin Society, Ancona, Italy
    • HEARN V. M., Escott G. M., Evans E. G. V. and Adams D. J. 1996. Chitinases of the cell surface and wall of Aspergillus fumigatus. In Chitin Enzymology. pp 261-72. Edited by R. A. A. Muzzarelli. European Chitin Society, Ancona, Italy.
    • (1996) Chitin Enzymology , pp. 261-272
    • Hearn, V.M.1    Escott, G.M.2    Evans, E.G.V.3    Adams, D.J.4
  • 17
    • 0029704305 scopus 로고    scopus 로고
    • Effects of tunicamycin on glycoprotein antigens of Aspergillus fumigatus
    • HEARN V. M. and Shimizu M. 1996. Effects of tunicamycin on glycoprotein antigens of Aspergillus fumigatus. Microbios 85: 239-50.
    • (1996) Microbios , vol.85 , pp. 239-250
    • Hearn, V.M.1    Shimizu, M.2
  • 18
    • 0006940014 scopus 로고    scopus 로고
    • Intracellular and wall-associated chitinases of Aspergillus fumigatus
    • Edited by S. Suzuki and M. Suzuki. Saikon Publishing Co., Ltd, Tokyo, Japan
    • HEARN V. M., Escott G. M., Evans E. G. V. and Adams D. J. 1997. Intracellular and wall-associated chitinases of Aspergillus fumigatus. In Fungal Cells in Biodefense Mechanism. pp 247-52. Edited by S. Suzuki and M. Suzuki. Saikon Publishing Co., Ltd, Tokyo, Japan.
    • (1997) Fungal Cells in Biodefense Mechanism , pp. 247-252
    • Hearn, V.M.1    Escott, G.M.2    Evans, E.G.V.3    Adams, D.J.4
  • 19
    • 0026063240 scopus 로고
    • A 58-kDa resident protein of the cis Golgi cisterna is not terminally glycosylated
    • HENDRICKS L. C., Gabel C. A., Suh K. and Farquar M. G. 1991. A 58-kDa resident protein of the cis Golgi cisterna is not terminally glycosylated. J. biol. Chem. 266 17559-65.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17559-17565
    • Hendricks, L.C.1    Gabel, C.A.2    Suh, K.3    Farquar, M.G.4
  • 20
    • 0024424147 scopus 로고
    • Purification and properties cytochrome P-450-dependent 14α-sterol demethylase from Candida albicans
    • HITCHCOCK C. A., Dickinson K., Brown S. B., Evans E. G. V. and Adams D. J. 1989. Purification and properties cytochrome P-450-dependent 14α-sterol demethylase from Candida albicans. Biochem. J. 263 573-9.
    • (1989) Biochem. J. , vol.263 , pp. 573-579
    • Hitchcock, C.A.1    Dickinson, K.2    Brown, S.B.3    Evans, E.G.V.4    Adams, D.J.5
  • 21
    • 0025945169 scopus 로고
    • Oligosaccharides at each glycosylation site make structure-dependent contributions to biological properties of human tissue plasminogen activator
    • HOWARD S. H., Wittwer A. J. and Welply J. K. 1991. Oligosaccharides at each glycosylation site make structure-dependent contributions to biological properties of human tissue plasminogen activator. Glycobiology 1 411-7.
    • (1991) Glycobiology , vol.1 , pp. 411-417
    • Howard, S.H.1    Wittwer, A.J.2    Welply, J.K.3
  • 22
    • 0028944878 scopus 로고
    • Conformational implications of asparagine-linked glycosylation
    • IMPERIALI B. and Rickert K. W. 1995. Conformational implications of asparagine-linked glycosylation. Proc. natn. Acad Sci. U.S.A. 92 97-101.
    • (1995) Proc. Natn. Acad Sci. U.S.A. , vol.92 , pp. 97-101
    • Imperiali, B.1    Rickert, K.W.2
  • 23
    • 0021380190 scopus 로고
    • Purification and characterization of two biosynthetic intermediates of ovalbumin
    • KATO Y., Iwase H. and Hotta K. 1984. Purification and characterization of two biosynthetic intermediates of ovalbumin. J. Biochem. 95 455-63.
    • (1984) J. Biochem. , vol.95 , pp. 455-463
    • Kato, Y.1    Iwase, H.2    Hotta, K.3
  • 24
    • 0000234469 scopus 로고
    • Several 'pathogenesis-related' proteins in potato are 1,3-β-glucanases and chitinases
    • KOMBRINK E., Schroder M. and Hahlbrock K. 1988. Several 'pathogenesis-related' proteins in potato are 1,3-β-glucanases and chitinases. Proc. natn. Acad. Sci. U.S.A. 85 782-6.
    • (1988) Proc. Natn. Acad. Sci. U.S.A. , vol.85 , pp. 782-786
    • Kombrink, E.1    Schroder, M.2    Hahlbrock, K.3
  • 25
    • 3643085093 scopus 로고
    • Ultrastructural localization of Aspergillus fumigatus antigens reacting with specific antibodies in aspergillosis
    • KURUP V. P., Reijula K. E. and Fink J. N. 1990. Ultrastructural localization of Aspergillus fumigatus antigens reacting with specific antibodies in aspergillosis. Abst. Am. Soc. Microbiol. p 417.
    • (1990) Abst. Am. Soc. Microbiol. , pp. 417
    • Kurup, V.P.1    Reijula, K.E.2    Fink, J.N.3
  • 26
    • 0028809398 scopus 로고
    • Preliminary characterization of the material released to the culture medium by Candida albicans yeast and mycelial cells
    • LOPEZ-RIBOT J. L., Gozalbo D., Sepulveda P., Casanova M. and Martinez J. P. 1995. Preliminary characterization of the material released to the culture medium by Candida albicans yeast and mycelial cells. Antonie Leeuwenhoek 68 195-201.
    • (1995) Antonie Leeuwenhoek , vol.68 , pp. 195-201
    • Lopez-Ribot, J.L.1    Gozalbo, D.2    Sepulveda, P.3    Casanova, M.4    Martinez, J.P.5
  • 27
    • 0028304284 scopus 로고
    • The purification and characterization of chitinase from Candida albicans
    • MELLOR K. J., Nicholas R. O. and Adams D. J. 1994. The purification and characterization of chitinase from Candida albicans. FEMS Microbiol. Letters 119 111-8.
    • (1994) FEMS Microbiol. Letters , vol.119 , pp. 111-118
    • Mellor, K.J.1    Nicholas, R.O.2    Adams, D.J.3
  • 28
    • 0023955543 scopus 로고
    • Secretion of an active nonglycosylated form of the repressible acid phosphatase of Saccharomyces cerevisiae in the presence of tunicamycin at low temperatures
    • MIZUNAGA T., Izawa M., Ikeda K. and Mamyama Y. 1988. Secretion of an active nonglycosylated form of the repressible acid phosphatase of Saccharomyces cerevisiae in the presence of tunicamycin at low temperatures. J. Biochem. 103 321-6.
    • (1988) J. Biochem. , vol.103 , pp. 321-326
    • Mizunaga, T.1    Izawa, M.2    Ikeda, K.3    Mamyama, Y.4
  • 29
    • 0014540906 scopus 로고
    • The chitinase of Serratia marcescens
    • MONREAL J. and Reese E. T. 1969. The chitinase of Serratia marcescens. Can. J. Microbiol. 15 689-96.
    • (1969) Can. J. Microbiol. , vol.15 , pp. 689-696
    • Monreal, J.1    Reese, E.T.2
  • 30
    • 0016188189 scopus 로고
    • A role of the carbohydrate moiety of glucose oxidase: Kinetic evidence for protection of the enzyme from thermal inactivation in the presence of sodium dodecyl sulfate
    • NAKAMURA S. and Hayashi S. 1974. A role of the carbohydrate moiety of glucose oxidase: kinetic evidence for protection of the enzyme from thermal inactivation in the presence of sodium dodecyl sulfate. FEBS Letters 41 327-30.
    • (1974) FEBS Letters , vol.41 , pp. 327-330
    • Nakamura, S.1    Hayashi, S.2
  • 32
    • 0000859095 scopus 로고
    • A technique for detection of chitinase, β-1,3-glucanase, and protein patterns after a single separation using polyacrylamide gel electrophoresis or isoelectrofocusing
    • PAN S. Q., Ye X. S. and Kuc J. 1991. A technique for detection of chitinase, β-1,3-glucanase, and protein patterns after a single separation using polyacrylamide gel electrophoresis or isoelectrofocusing. Phytopathology 81 970-4.
    • (1991) Phytopathology , vol.81 , pp. 970-974
    • Pan, S.Q.1    Ye, X.S.2    Kuc, J.3
  • 33
    • 0018174484 scopus 로고
    • Distribution of autolysins in hyphae of Aspergillus nidulans: Evidence for a lipid-mediated attachment to hyphal walls
    • POLACHECK I. and Rosenberger R. F. 1978. Distribution of autolysins in hyphae of Aspergillus nidulans: evidence for a lipid-mediated attachment to hyphal walls. J. Bact. 135 741-7.
    • (1978) J. Bact. , vol.135 , pp. 741-747
    • Polacheck, I.1    Rosenberger, R.F.2
  • 34
    • 0025933474 scopus 로고
    • The 43-kDa glycoprotein from the human pathogen Paracoccidioides brasiliensis and its deglycosylated form: Excretion and susceptibility to proteolysis
    • PUCCIA R. and Travassos L. R. 1991. The 43-kDa glycoprotein from the human pathogen Paracoccidioides brasiliensis and its deglycosylated form: excretion and susceptibility to proteolysis. Archs. Biochem. Biophys. 289 298-302.
    • (1991) Archs. Biochem. Biophys. , vol.289 , pp. 298-302
    • Puccia, R.1    Travassos, L.R.2
  • 35
    • 0027006764 scopus 로고
    • Thyroid peroxidase glycosylation: The location and nature of the N-linked oligosaccharide units in porcine thyroid peroxidase
    • RAWITCH A. B., Pollock O., Yang S. X. and Taurog A. 1992. Thyroid peroxidase glycosylation: the location and nature of the N-linked oligosaccharide units in porcine thyroid peroxidase. Archs. Biochem. Biophys. 297 321-7.
    • (1992) Archs. Biochem. Biophys. , vol.297 , pp. 321-327
    • Rawitch, A.B.1    Pollock, O.2    Yang, S.X.3    Taurog, A.4
  • 36
    • 0024696560 scopus 로고
    • Endochitinase from Aspergillus nidulans implicated in the autolysis of its cell wall
    • REYES F., Calatayud J. and Martinez M. J. 1989. Endochitinase from Aspergillus nidulans implicated in the autolysis of its cell wall. FEMS Microbiol. Letters 60 119-24.
    • (1989) FEMS Microbiol. Letters , vol.60 , pp. 119-124
    • Reyes, F.1    Calatayud, J.2    Martinez, M.J.3
  • 37
    • 0023473794 scopus 로고
    • Rapid isoelectric focusing in vertical polyacrylamide minigel system
    • ROBERTSON E. F., Dannelly H. K., Malloy P. J. and Reeves H. C. 1987. Rapid isoelectric focusing in vertical polyacrylamide minigel system. Analyt. Biochem. 167 290-4.
    • (1987) Analyt. Biochem. , vol.167 , pp. 290-294
    • Robertson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeves, H.C.4
  • 39
    • 0028310326 scopus 로고
    • Segmental differentiation of permeability, protein glycosylation, and morphology of cultured bovine lung vascular endothelium
    • SCHNITZER J. E., Siflinger-Birnboim A., Del Vecchio P. J. and Malik A. B. 1994. Segmental differentiation of permeability, protein glycosylation, and morphology of cultured bovine lung vascular endothelium. Biochem. biophys. Res. Commun. 199 11-9.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 11-19
    • Schnitzer, J.E.1    Siflinger-Birnboim, A.2    Del Vecchio, P.J.3    Malik, A.B.4
  • 40
    • 0002593051 scopus 로고
    • Entopathogenic isolates of Metarhizium anisopliae, Beauveria bassiana and Aspergillus flavus produce multiple extracellular chitinase isoenzymes
    • ST LEGER R. J., Staples R. C. and Roberts D. W. 1993. Entopathogenic isolates of Metarhizium anisopliae, Beauveria bassiana and Aspergillus flavus produce multiple extracellular chitinase isoenzymes. J. Invert. Path. 61 81-4.
    • (1993) J. Invert. Path. , vol.61 , pp. 81-84
    • St Leger, R.J.1    Staples, R.C.2    Roberts, D.W.3
  • 41
    • 0016475460 scopus 로고
    • Serological cross-reactivity of the D-galacto-D-mannans isolated from several pathogenic fungi against anti-Hormodendrum pedrosi sera
    • SUZUKI S. and Takeda N. 1975. Serological cross-reactivity of the D-galacto-D-mannans isolated from several pathogenic fungi against anti-Hormodendrum pedrosi sera. Carbohydr. Res. 40 193-7.
    • (1975) Carbohydr. Res. , vol.40 , pp. 193-197
    • Suzuki, S.1    Takeda, N.2
  • 42
    • 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. natn. Acad. Sci. U.S.A. 76 4350-4.
    • (1979) Proc. Natn. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 43
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • TRUDEL J. and Asselin A. 1989. Detection of chitinase activity after polyacrylamide gel electrophoresis. Analyt. Biochem. 178 362-6.
    • (1989) Analyt. Biochem. , vol.178 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 44
    • 0000966280 scopus 로고
    • Distribution of lysine pathways among fungi; evolutionary implications
    • VOGEL H. I. 1964. Distribution of lysine pathways among fungi; evolutionary implications. Am. Naturalist 98 435-46.
    • (1964) Am. Naturalist , vol.98 , pp. 435-446
    • Vogel, H.I.1
  • 45
    • 0020680671 scopus 로고
    • Use of Aspergillus fumigatus mycelial antigens in enzyme-linked immunosorbent assay and counter-immunoelectrophoresis
    • WILSON E. V. and Hearn V. M. 1983. Use of Aspergillus fumigatus mycelial antigens in enzyme-linked immunosorbent assay and counter-immunoelectrophoresis. J. med Microbiol. 16 97-105.
    • (1983) J. Med Microbiol. , vol.16 , pp. 97-105
    • Wilson, E.V.1    Hearn, V.M.2
  • 46
    • 0030220095 scopus 로고    scopus 로고
    • The structural role of sugars in glycoproteins
    • WYSS D. F. and Wagner O. 1996. The structural role of sugars in glycoproteins. Curr. Opin. Biotechnol. 7 409-16.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 409-416
    • Wyss, D.F.1    Wagner, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.