메뉴 건너뛰기




Volumn 126, Issue 1, 1999, Pages 26-33

Amino acid sequence and some properties of phytolacain R, a cysteine protease from full-growth fruits of pokeweed, Phytolacca americana

Author keywords

Amino acid sequence; Cysteine protease; Endopeptidase; Phytolacca americana; Pokeweed

Indexed keywords

ACTINIDIN; ALANINE; BRINASE; BROMELAIN; CHYMOTRYPSIN; CYANOGEN BROMIDE; CYSTEINE PROTEINASE; GLYCINE; HISTIDINE; METHIONINE; PAPAIN; PHENYLALANINE; PROLINE; TRYPSIN; TRYPTOPHAN; TYROSINE; VALINE;

EID: 0032820179     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022431     Document Type: Article
Times cited : (2)

References (25)
  • 2
    • 0007684644 scopus 로고
    • Isolation and characterization of a protease from Phytolacca americana
    • Kaneda, M., Izumi, S., Fukuda, T., Uchikoba, T., and Tominaga, N. (1988) Isolation and characterization of a protease from Phytolacca americana. Phytochemistry 27, 3661-3662
    • (1988) Phytochemistry , vol.27 , pp. 3661-3662
    • Kaneda, M.1    Izumi, S.2    Fukuda, T.3    Uchikoba, T.4    Tominaga, N.5
  • 3
    • 0029328533 scopus 로고
    • Comparison of phytolacain R, a cysteine protease from Phytolacca americana, with papain
    • Kaneda, M., Nagatome, S., and Uchikoba, T. (1995) Comparison of phytolacain R, a cysteine protease from Phytolacca americana, with papain. Phytochemistry 39, 997-999
    • (1995) Phytochemistry , vol.39 , pp. 997-999
    • Kaneda, M.1    Nagatome, S.2    Uchikoba, T.3
  • 4
    • 0032176218 scopus 로고    scopus 로고
    • Comparison of phytolacain G, a cysteine protease from Phytolacca americana, with phytolacain R
    • Uchikoba, T., Yonezawa, H., Shimada, M., and Kaneda, M. (1998) Comparison of phytolacain G, a cysteine protease from Phytolacca americana, with phytolacain R. Biosci. Biotech. Biochem. 62, 2058-2061
    • (1998) Biosci. Biotech. Biochem. , vol.62 , pp. 2058-2061
    • Uchikoba, T.1    Yonezawa, H.2    Shimada, M.3    Kaneda, M.4
  • 5
    • 0001830556 scopus 로고
    • Roles of proteolytic enzymes in interactions of plants with other organism
    • Dalling, M.J., ed. CRC Press, Florida
    • Boiler, T. (1986) Roles of proteolytic enzymes in interactions of plants with other organism in Plant Proteolytic Enzymes (Dalling, M.J., ed.) Vol. 1, pp. 67 96, CRC Press, Florida
    • (1986) Plant Proteolytic Enzymes , vol.1 , pp. 6796
    • Boiler, T.1
  • 6
    • 0000795704 scopus 로고
    • Crystalline soybean trypsin inhibitor
    • Kunitz, M. (1947) Crystalline soybean trypsin inhibitor. J. Gen. Physiol. 30, 291-310
    • (1947) J. Gen. Physiol. , vol.30 , pp. 291-310
    • Kunitz, M.1
  • 7
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 8
    • 33749946901 scopus 로고
    • Colorimatric method for determination of sugars and related substances
    • Dubois, M., Gilles, K.A., Hamilton, J.K., Robert, P.A., and Smith, F. (1956) Colorimatric method for determination of sugars and related substances. Anal. Chem. 28, 350-356
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Robert, P.A.4    Smith, F.5
  • 9
    • 0017729399 scopus 로고
    • Reductive cleavage of cysteine disulfides with tributylphosphine
    • Hirs, C.H.W. and Timacheff, S.N., eds. Academic Press, New York
    • Ruegg, U.T. and Rudinger, J. (1977) Reductive cleavage of cysteine disulfides with tributylphosphine in Methods in Enzymology (Hirs, C.H.W. and Timacheff, S.N., eds.) Vol. 47, pp. 111-116, Academic Press, New York
    • (1977) Methods in Enzymology , vol.47 , pp. 111-116
    • Ruegg, U.T.1    Rudinger, J.2
  • 10
    • 0001830556 scopus 로고
    • Roles of proteolytic enzymes in interactions of plants with other organisms
    • Dalling, M.J., ed. CRC Press, Florida
    • Boller, T. (1986) Roles of proteolytic enzymes in interactions of plants with other organisms in Plant Proteolytic Enzymes (Dalling, M.J., ed.) Vol. 1, pp. 67-96, CRC Press, Florida
    • (1986) Plant Proteolytic Enzymes , vol.1 , pp. 67-96
    • Boller, T.1
  • 11
    • 0002583432 scopus 로고
    • Activation of conventional S-protecting groups of cysteine by conversion into the 3-nitro-2-pyridinesulfenyl (Npys) group
    • Matsueda, R., Umeyama, H., Kominami, E., and Katunuma, N. (1988) Activation of conventional S-protecting groups of cysteine by conversion into the 3-nitro-2-pyridinesulfenyl (Npys) group. Chem. Lett. 1857-1860
    • (1988) Chem. Lett. , pp. 1857-1860
    • Matsueda, R.1    Umeyama, H.2    Kominami, E.3    Katunuma, N.4
  • 14
    • 0022828086 scopus 로고
    • Cloning and sequencing of papain encoding cDNA
    • Cohen, L.W., Coghlan, V.M., and Dihel, L.C. (1986) Cloning and sequencing of papain encoding cDNA. Gene 48, 219-227
    • (1986) Gene , vol.48 , pp. 219-227
    • Cohen, L.W.1    Coghlan, V.M.2    Dihel, L.C.3
  • 15
    • 0017846050 scopus 로고
    • The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis
    • Carne, A. and Moore, C.H. (1978) The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis. Biochem. J. 173, 73-83
    • (1978) Biochem. J. , vol.173 , pp. 73-83
    • Carne, A.1    Moore, C.H.2
  • 16
    • 0024551586 scopus 로고
    • Stem bromelain; amino acid sequence and implications for weak binding of cystatin
    • Ritonja, A., Rowan, A.D., Buttle, D.J., Rawlings, N.D., Turk, V., and Barrett, A.J. (1989) Stem bromelain; amino acid sequence and implications for weak binding of cystatin. FEBS Lett. 247, 419-424
    • (1989) FEBS Lett. , vol.247 , pp. 419-424
    • Ritonja, A.1    Rowan, A.D.2    Buttle, D.J.3    Rawlings, N.D.4    Turk, V.5    Barrett, A.J.6
  • 17
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Barrett, A.J., ed. Academic Press, New York
    • Rawlings, N.D. and Barrett, A.J. (1994) Families of cysteine peptidases in Methods in Enzymology (Barrett, A.J., ed.) Vol. 244, pp. 461-486, Academic Press, New York
    • (1994) Methods in Enzymology , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 18
    • 0024669731 scopus 로고
    • The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain
    • Jacquet, A., Kleinschmidt, T., Schnek, A.G., Looze, Y., and Braunitzer, G. (1989) The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain. Biol. Chem. Hoppe-Seyler 370, 425-434
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 425-434
    • Jacquet, A.1    Kleinschmidt, T.2    Schnek, A.G.3    Looze, Y.4    Braunitzer, G.5
  • 19
    • 0024066667 scopus 로고
    • The thiol proteinases from the latex of Carica papaya L. II. The primary structure of Proteinase Ω
    • Dubois, T., Kleinschmidt, T., Schnek, A.G., Looze, Y., and Braunitzer, G. (1988) The thiol proteinases from the latex of Carica papaya L. II. The primary structure of Proteinase Ω. Biol. Chem. Hoppe-Seyler 369, 741-754
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 741-754
    • Dubois, T.1    Kleinschmidt, T.2    Schnek, A.G.3    Looze, Y.4    Braunitzer, G.5
  • 20
    • 0024523512 scopus 로고
    • The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain
    • Kowlessur, D., O'Driscoll, M., Topham, C.M., Templeton, W., Thomas, E.W., and Brocklehurst, K. (1989) The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain. Biochem. J. 259, 443-452
    • (1989) Biochem. J. , vol.259 , pp. 443-452
    • Kowlessur, D.1    O'Driscoll, M.2    Topham, C.M.3    Templeton, W.4    Thomas, E.W.5    Brocklehurst, K.6
  • 21
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analogues to crystalline papain
    • Drenth, J., Kalk, K.H., and Swen, H.M. (1976) Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 15, 3731-3738
    • (1976) Biochemistry , vol.15 , pp. 3731-3738
    • Drenth, J.1    Kalk, K.H.2    Swen, H.M.3
  • 23
    • 0021672206 scopus 로고
    • L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide - A chromogenic substrate for thiol protease assay
    • Filippova, I.Y., Lysogorskaya, E.N., Oksenoit, E.S., Rudenskaya, G.N., and Stepanov, V.M. (1984) L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide - A chromogenic substrate for thiol protease assay. Anal. Biochem. 143, 293-297
    • (1984) Anal. Biochem. , vol.143 , pp. 293-297
    • Filippova, I.Y.1    Lysogorskaya, E.N.2    Oksenoit, E.S.3    Rudenskaya, G.N.4    Stepanov, V.M.5
  • 24
    • 0028446499 scopus 로고
    • Primary structure of CC-III. The glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook
    • Jaziri, M., Kleinschmidt, T., Walraevens, V., Schnek, A.G., and Looze, Y. (1994) Primary structure of CC-III. The glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook. Biol. Chem. Hoppe-Seyler 375, 379-385
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 379-385
    • Jaziri, M.1    Kleinschmidt, T.2    Walraevens, V.3    Schnek, A.G.4    Looze, Y.5
  • 25
    • 0027690396 scopus 로고
    • Fruit developmental regulation of the kiwifruit actinidin promoter is conserved in transgenic petunia plants
    • Lin, E., Burns, D.J.W., and Gardner, B.C. (1993) Fruit developmental regulation of the kiwifruit actinidin promoter is conserved in transgenic petunia plants. Plant Mol. Biol. 23, 489-499
    • (1993) Plant Mol. Biol. , vol.23 , pp. 489-499
    • Lin, E.1    Burns, D.J.W.2    Gardner, B.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.