메뉴 건너뛰기




Volumn 66, Issue 9, 2005, Pages 983-990

Grifolisin, a member of the sedolisin family produced by the fungus Grifola frondosa

Author keywords

Grifola frondosa; Grifolisin; Pepstatin; Proteinase; Sedolisin

Indexed keywords

CARBOXYPEPTIDASE; GRIFOLISIN, GRIFOLA FRONDOSA;

EID: 19344368324     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2005.02.014     Document Type: Article
Times cited : (14)

References (29)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 78651153791 scopus 로고
    • Disk electrophoresis II. Method and application to human serume proteins
    • B.J. Davis Disk electrophoresis II. Method and application to human serume proteins Ann. NY Acad. Sci. 121 1964 404 424
    • (1964) Ann. NY Acad. Sci. , vol.121 , pp. 404-424
    • Davis, B.J.1
  • 4
    • 0014939933 scopus 로고
    • The chromatographic determination of cystine and cysteins residues in proteina as S-β-(4-pyridylethyl)-cysteine
    • M. Friedman, H. Krull, and J.F. Cavins The chromatographic determination of cystine and cysteins residues in proteina as S-β-(4-pyridylethyl)- cysteine J. Biol. Chem. 254 1970 3868 3871
    • (1970) J. Biol. Chem. , vol.254 , pp. 3868-3871
    • Friedman, M.1    Krull, H.2    Cavins, J.F.3
  • 5
    • 84944043841 scopus 로고    scopus 로고
    • Aspergillopepsin I
    • second ed. A.J. Barrett N.D. Rawlings J.F. Woessner Elsevier Academic Press Amsterdam
    • E. Ichishima Aspergillopepsin I second ed. A.J. Barrett N.D. Rawlings J.F. Woessner Handbook of proteolytic enzymes vol. 1 2004 Elsevier Academic Press Amsterdam 92 96
    • (2004) Handbook of Proteolytic Enzymes , vol.1 , pp. 92-96
    • Ichishima, E.1
  • 6
    • 0033051346 scopus 로고    scopus 로고
    • Identification of carboxyl residues in pepstatin-insensitive carboxyl proteinase fromPseudomonas sp. 101 that participates in catalysis and substrate binding
    • M. Ito, S. Narutaki, K. Uchida, and K. Oda Identification of carboxyl residues in pepstatin-insensitive carboxyl proteinase fromPseudomonas sp. 101 that participates in catalysis and substrate binding J. Biochem. (Tokyo) 125 1999 210 216
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 210-216
    • Ito, M.1    Narutaki, S.2    Uchida, K.3    Oda, K.4
  • 7
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacterophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacterophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 9
    • 0035910463 scopus 로고    scopus 로고
    • The human CLN2 protein/ tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH
    • L. Lin, I. Sohar, H. Lackland, and P. Lobel The human CLN2 protein/ tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH J. Biol. Chem. 276 2001 2249 2255
    • (2001) J. Biol. Chem. , vol.276 , pp. 2249-2255
    • Lin, L.1    Sohar, I.2    Lackland, H.3    Lobel, P.4
  • 10
    • 0024492484 scopus 로고
    • Polymerase chain reaction with single-sided specificity: Analysis of T cell receptor δ chain
    • E.Y. Loh, J.F. Elliot, S. Cwirla, L.L. Lanier, and M.M. Davis Polymerase chain reaction with single-sided specificity: analysis of T cell receptor δ chain Science 243 1989 217 220
    • (1989) Science , vol.243 , pp. 217-220
    • Loh, E.Y.1    Elliot, J.F.2    Cwirla, S.3    Lanier, L.L.4    Davis, M.M.5
  • 11
    • 84954976476 scopus 로고
    • New acid proteases from Scytalidium lignicolum M-133
    • S. Murao, K. Oda, and Y. Matsushita New acid proteases from Scytalidium lignicolum M-133 Agric. Biol. Chem. 36 1972 1647 1650
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 1647-1650
    • Murao, S.1    Oda, K.2    Matsushita, Y.3
  • 12
    • 0027446449 scopus 로고
    • Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. NM-12
    • S. Murao, K. Ohkuni, M. Nagao, K. Hirayama, K. Fukuhara, K. Oda, H. Oyama, and T. Shin Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. NM-12 J. Biol. Chem. 268 1993 349 355
    • (1993) J. Biol. Chem. , vol.268 , pp. 349-355
    • Murao, S.1    Ohkuni, K.2    Nagao, M.3    Hirayama, K.4    Fukuhara, K.5    Oda, K.6    Oyama, H.7    Shin, T.8
  • 14
    • 0023154620 scopus 로고
    • Purification and properties of a pepstatin-insensitive carboxyl proteinase from Gram-negative bacterium
    • K. Oda, M. Sugitani, K. Fukuhara, and S. Murao Purification and properties of a pepstatin-insensitive carboxyl proteinase from Gram-negative bacterium Biochim. Biophys. Acta 923 1987 463 469
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 463-469
    • Oda, K.1    Sugitani, M.2    Fukuhara, K.3    Murao, S.4
  • 15
    • 0000916308 scopus 로고
    • A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases
    • K. Oda, Y. Fukuda, S. Muro, K. Uchida, and M. Kinoshita A novel proteinase inhibitor, tyrostatin, inhibiting some pepstatin-insensitive carboxyl proteinases Agric. Biol. Chem. 53 1989 405 415
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 405-415
    • Oda, K.1    Fukuda, Y.2    Muro, S.3    Uchida, K.4    Kinoshita, M.5
  • 16
    • 0028046586 scopus 로고
    • Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101
    • K. Oda, T. Takahashi, Y. Tokuda, Y. Shibano, and S. Takahashi Cloning, nucleotide sequence, and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Pseudomonas sp. 101 J. Biol. Chem. 269 1994 26518 26524
    • (1994) J. Biol. Chem. , vol.269 , pp. 26518-26524
    • Oda, K.1    Takahashi, T.2    Tokuda, Y.3    Shibano, Y.4    Takahashi, S.5
  • 17
    • 0029761009 scopus 로고    scopus 로고
    • Cloning and expression of an isovaleryl pepstatin-insensitive carboxylproteinase gene from Xanthomonas sp. T-22
    • K. Oda, M. Ito, K. Uchida, Y. Shibano, K. Fukuhara, and S. Takahashi Cloning and expression of an isovaleryl pepstatin-insensitive carboxylproteinase gene from Xanthomonas sp. T-22 J. Biochem. (Tokyo) 120 1996 564 572
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 564-572
    • Oda, K.1    Ito, M.2    Uchida, K.3    Shibano, Y.4    Fukuhara, K.5    Takahashi, S.6
  • 18
    • 0003327572 scopus 로고
    • One-sided polymerase chain reaction: The amplification of cDNA
    • O. Ohara, R.L. Dorit, and W. Gilbert One-sided polymerase chain reaction: the amplification of cDNA Proc. Natl. Acad. Sci. USA 86 1989 5673 5677
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5673-5677
    • Ohara, O.1    Dorit, R.L.2    Gilbert, W.3
  • 19
    • 0033600764 scopus 로고    scopus 로고
    • Identification of catalytic residues of pepstatin-insensitive carboxyl proteinase from prokaryotes by site-directed mutagenesis
    • H. Oyama, S. Abe, S. Uchiyama, S. Takahashi, and K. Oda Identification of catalytic residues of pepstatin-insensitive carboxyl proteinase from prokaryotes by site-directed mutagenesis J. Biol. Chem. 274 1996 27815 27822
    • (1996) J. Biol. Chem. , vol.274 , pp. 27815-27822
    • Oyama, H.1    Abe, S.2    Uchiyama, S.3    Takahashi, S.4    Oda, K.5
  • 20
    • 19344378833 scopus 로고    scopus 로고
    • Objective and strategy in enzyme purification
    • third ed. Oxford University Press Oxford
    • N.C. Price, and L. Stevens Objective and strategy in enzyme purification Fundamentals of enzymology third ed. 1999 Oxford University Press Oxford 16
    • (1999) Fundamentals of Enzymology , pp. 16
    • Price, N.C.1    Stevens, L.2
  • 21
    • 0032897884 scopus 로고    scopus 로고
    • Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis
    • N.D. Rawlings, and A.J. Barrett Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis Biochim. Biophys. Acta 1429 1999 496 500
    • (1999) Biochim. Biophys. Acta , vol.1429 , pp. 496-500
    • Rawlings, N.D.1    Barrett, A.J.2
  • 22
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases. I. Papain Biochem. Biophys. Res. Commun. 7 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.7 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 23
    • 0030866233 scopus 로고    scopus 로고
    • Association of mutations in a lysosomal protein with classical 23 late-infantile neuronal ceroid lipofuscinosis
    • D.E. Sleat, R.J. Donnelly, H. Lackland, C.G. Lui, I. Sohar, R.K. Pullarkat, and P. Lobel Association of mutations in a lysosomal protein with classical 23 late-infantile neuronal ceroid lipofuscinosis Science 277 1997 1802 1805
    • (1997) Science , vol.277 , pp. 1802-1805
    • Sleat, D.E.1    Donnelly, R.J.2    Lackland, H.3    Lui, C.G.4    Sohar, I.5    Pullarkat, R.K.6    Lobel, P.7
  • 24
    • 84953965833 scopus 로고
    • Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum
    • T. Terashita, K. Oda, M. Kono, and S. Murao Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum Agric. Biol. Chem. 48 1984 1029 1035
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1029-1035
    • Terashita, T.1    Oda, K.2    Kono, M.3    Murao, S.4
  • 25
    • 0040388396 scopus 로고
    • Purification and some properties of carboxyl proteinase in extract from Lentinus edodes fruit-body
    • T. Terashita, K. Oda, M. Kono, and S. Murao Purification and some properties of carboxyl proteinase in extract from Lentinus edodes fruit-body Agric. Biol. Chem. 48 1984 2639 2645
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 2639-2645
    • Terashita, T.1    Oda, K.2    Kono, M.3    Murao, S.4
  • 26
    • 0023046815 scopus 로고
    • A new method for predicting sequence cleavage sites
    • G. von Heijne A new method for predicting sequence cleavage sites Nucleic Acids Res. 14 1986 4683 4690
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 28
    • 0037779903 scopus 로고    scopus 로고
    • Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases
    • A. Wlodawer, M. Li, A. Gustchina, H. Oyama, B.M. Dunn, and K. Oda Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases Acta Biochim. Polon. 50 2003 81 102
    • (2003) Acta Biochim. Polon. , vol.50 , pp. 81-102
    • Wlodawer, A.1    Li, M.2    Gustchina, A.3    Oyama, H.4    Dunn, B.M.5    Oda, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.