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Volumn 87, Issue 4, 1999, Pages 418-423

Cloning and expression of chitin deacetylase gene from a deuteromycete, Colletotrichum lindemuthianum

Author keywords

Chitin deacetylase; Colletotrichum lindernuthianum

Indexed keywords

CHITIN DERIVATIVE;

EID: 0032912912     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(99)80088-7     Document Type: Article
Times cited : (30)

References (17)
  • 1
    • 0002714889 scopus 로고
    • Production and application of chitin and chitosan in Japan
    • Skjåk-Bræk, G., Anthonsen, T., and Sandford, P. (ed.). Elsevier Applied Science, London and New York
    • 1. Hirano, S.: Production and application of chitin and chitosan in Japan, p. 37-43. In Skjåk-Bræk, G., Anthonsen, T., and Sandford, P. (ed.), Chitin and chitosan. Elsevier Applied Science, London and New York (1989).
    • (1989) Chitin and Chitosan , pp. 37-43
    • Hirano, S.1
  • 2
    • 0021189336 scopus 로고
    • Characterization of the smallest chitosan oligomer that is maximally antifungal to Fusarium solani and elicits pisatin formation in Pisum sativum
    • 2. Kendra, D. F. and Hadwiger, L. A.: Characterization of the smallest chitosan oligomer that is maximally antifungal to Fusarium solani and elicits pisatin formation in Pisum sativum. Exp. Mycol., 8, 276-281 (1984).
    • (1984) Exp. Mycol. , vol.8 , pp. 276-281
    • Kendra, D.F.1    Hadwiger, L.A.2
  • 4
    • 0029113381 scopus 로고
    • Chitin deacetylation by enzymatic means: Monitoring of deacetylation process
    • 4. Martinou, A., Kafetzopoulos, D., and Bouriotis, V.: Chitin deacetylation by enzymatic means: monitoring of deacetylation process. Carbohydr. Res., 273, 235-242 (1995).
    • (1995) Carbohydr. Res. , vol.273 , pp. 235-242
    • Martinou, A.1    Kafetzopoulos, D.2    Bouriotis, V.3
  • 5
    • 0030267953 scopus 로고    scopus 로고
    • Purification and characterization of extracellular chitin deacetylase from Colletotrichum lindemuthianum
    • 5. Tokuyasu, K., Ohnishi-Kameyama, M., and Hayashi, K.: Purification and characterization of extracellular chitin deacetylase from Colletotrichum lindemuthianum. Biosci. Botech. Biochem., 60, 1598-1603 (1996).
    • (1996) Biosci. Botech. Biochem. , vol.60 , pp. 1598-1603
    • Tokuyasu, K.1    Ohnishi-Kameyama, M.2    Hayashi, K.3
  • 6
    • 0030731624 scopus 로고    scopus 로고
    • Deacetylation of chitin oligosaccharides of dp 2-4 by chitin deacetylase from Colletotrichum lindemuthianum
    • 6. Tokuyasu, K., Ono, H., Ohnishi-Kameyama, M., Hayashi, K., and Mori, Y.: Deacetylation of chitin oligosaccharides of dp 2-4 by chitin deacetylase from Colletotrichum lindemuthianum. Carbohydr. Res., 303, 353-358 (1997).
    • (1997) Carbohydr. Res. , vol.303 , pp. 353-358
    • Tokuyasu, K.1    Ono, H.2    Ohnishi-Kameyama, M.3    Hayashi, K.4    Mori, Y.5
  • 7
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • 7. Murray, M. G. and Thompson, W. F.: Rapid isolation of high molecular weight plant DNA. Nucl. Acids Res., 8, 4321-4325 (1980).
    • (1980) Nucl. Acids Res. , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 8
    • 0016207067 scopus 로고
    • Ribonucleic acid isolated by cesium chloride centrifugation
    • 8. Glisin, V., Crkvenjakov, R., and Byus, C.: Ribonucleic acid isolated by cesium chloride centrifugation. Biochemistry, 13, 2633 (1974).
    • (1974) Biochemistry , vol.13 , pp. 2633
    • Glisin, V.1    Crkvenjakov, R.2    Byus, C.3
  • 11
    • 0023920896 scopus 로고
    • Large-scale chromatography of recombinant proteins
    • 11. Hochuli, E: Large-scale chromatography of recombinant proteins. J. Chromatogr., 444, 293-302 (1988).
    • (1988) J. Chromatogr. , vol.444 , pp. 293-302
    • Hochuli, E.1
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 12. Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • 13. von Heijine, G.: Signal sequences. The limits of variation. J. Mol. Biol., 184, 99-105 (1985).
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijine, G.1
  • 14
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long-sought dibasic processing endoproteases
    • 14. Barr, P. J.: Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell., 66, 1-3 (1991).
    • (1991) Cell. , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 15
    • 0027219468 scopus 로고
    • The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products
    • 15. Kafetzopoulos, D., Thireos, G., Vournakis, J. N., and Bouriotis, V.: The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products. Proc. Natl. Acad. Sci. USA, 90, 8005-8008 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8005-8008
    • Kafetzopoulos, D.1    Thireos, G.2    Vournakis, J.N.3    Bouriotis, V.4
  • 16
    • 0022589864 scopus 로고
    • DNA sequence of Rhizobium trifolii nodulation genes reveals a reiterated and potentially regulatory sequence preceding nodABC and nodFE
    • 16. Schofield, P. R. and Wartson, J. M.: DNA sequence of Rhizobium trifolii nodulation genes reveals a reiterated and potentially regulatory sequence preceding nodABC and nodFE. Nucl. Acids Res., 14, 2891-2903 (1986).
    • (1986) Nucl. Acids Res. , vol.14 , pp. 2891-2903
    • Schofield, P.R.1    Wartson, J.M.2
  • 17
    • 0001030033 scopus 로고
    • Chitin deacetylase in cucumber leaves infected by Colletotrichum lagenarium
    • 17. Siegrist, J. and Kauss, H.: Chitin deacetylase in cucumber leaves infected by Colletotrichum lagenarium. Physiol. Mol. Plant Pathol., 36, 267-275 (1990).
    • (1990) Physiol. Mol. Plant Pathol. , vol.36 , pp. 267-275
    • Siegrist, J.1    Kauss, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.