메뉴 건너뛰기




Volumn 119, Issue 6, 1996, Pages 1106-1113

Purification, characterization, and sequencing of two cysteine proteinase inhibitors, Sca and Scb, from sunflower (Helianthus annuus) seeds

Author keywords

Amino acid sequence; Cysteine proteinase inhibitor; Helianthus annuus; Phytocystatin; Sunflower

Indexed keywords

CATHEPSIN H; CYSTATIN; CYSTEINE PROTEINASE INHIBITOR; FICIN; PAPAIN;

EID: 0029899115     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021355     Document Type: Article
Times cited : (41)

References (30)
  • 2
    • 84954967222 scopus 로고
    • Purification of a cysteine proteinase inhibitor from rice, Oryza sativa L. japonica
    • Abe, K. and Arai, S. (1985) Purification of a cysteine proteinase inhibitor from rice, Oryza sativa L. japonica. Agric. Biol. Chem. 49, 3349 3350
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 3349-3350
    • Abe, K.1    Arai, S.2
  • 3
    • 85004645817 scopus 로고
    • Purification and characterization of a rice cysteine proteinase inhibitor
    • Abe, K., Kondo, H., and Arai, S. (1987) Purification and characterization of a rice cysteine proteinase inhibitor. Agric. Biol. Chem. 51, 2763 2768
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2763-2768
    • Abe, K.1    Kondo, H.2    Arai, S.3
  • 4
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin)
    • Abe, K., Emori, Y., Kondo, H., Suzuki, K., and Arai, S. (1987) Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin). J. Biol. Chem. 262, 16793-16797
    • (1987) J. Biol. Chem. , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 5
    • 0025160575 scopus 로고
    • Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases
    • Kondo, H., Abe, K., Nishimura, I., Watanabe, H., Emori, Y., and Arai, S. (1990) Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. J. Biol. Chem. 265, 15832 15837
    • (1990) J. Biol. Chem. , vol.265 , pp. 15832-15837
    • Kondo, H.1    Abe, K.2    Nishimura, I.3    Watanabe, H.4    Emori, Y.5    Arai, S.6
  • 7
    • 0027368646 scopus 로고
    • The primary structure of inhibitor of cysteine proteinases from potato
    • Krizaj, I., Drobnic-Kosorok, M., Brzin, J., Jerala, R., and Turk, V. (1993) The primary structure of inhibitor of cysteine proteinases from potato. FEBS Lett. 333, 15 20
    • (1993) FEBS Lett. , vol.333 , pp. 15-20
    • Krizaj, I.1    Drobnic-Kosorok, M.2    Brzin, J.3    Jerala, R.4    Turk, V.5
  • 8
    • 0029447431 scopus 로고
    • Primary structure of a cysteine proteinase inhibitor from the fruit of avocado (Persea americana Mill)
    • Kimura, M., Ikeda, T., Fukumoto, D., Yamasaki, N., and Yonekura, M. (1995) Primary structure of a cysteine proteinase inhibitor from the fruit of avocado (Persea americana Mill). Biosci. Biotech. Biochem. 59, 2328 2329
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 23282329
    • Kimura, M.1    Ikeda, T.2    Fukumoto, D.3    Yamasaki, N.4    Yonekura, M.5
  • 10
    • 0026497716 scopus 로고
    • Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin
    • Abe, M., Abe, K., Kuroda, M., and Arai, S. (1992) Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Ear. J. Biochem. 209, 933-937
    • (1992) Ear. J. Biochem. , vol.209 , pp. 933-937
    • Abe, M.1    Abe, K.2    Kuroda, M.3    Arai, S.4
  • 11
    • 0021360655 scopus 로고
    • Separation and properties of three forms of cathepsin H-like cysteine proteinase from rat spleen
    • Yamamoto, K., Kamata, O., and Kato, Y. (1984) Separation and properties of three forms of cathepsin H-like cysteine proteinase from rat spleen. J. Biochem. 95, 477 484
    • (1984) J. Biochem. , vol.95 , pp. 477-484
    • Yamamoto, K.1    Kamata, O.2    Kato, Y.3
  • 12
    • 0001619034 scopus 로고
    • Characterization of rat spleen cathepsin B and different effects of anti-inflammatory drugs on its activity
    • Yamamoto, K., Kamata, O., Takeda, M., and Kato, Y. (1983) Characterization of rat spleen cathepsin B and different effects of anti-inflammatory drugs on its activity. Jpn. J. Oral Biol. 25, 834 838
    • (1983) Jpn. J. Oral Biol. , vol.25 , pp. 834-838
    • Yamamoto, K.1    Kamata, O.2    Takeda, M.3    Kato, Y.4
  • 13
    • 0022394161 scopus 로고
    • Characteristics of activation of cathepsin B by sodium salicylate and comparison of catalytic site properties of cathepsin B and H
    • Yamamoto, K., Takeda, M., and Kato, Y. (1985) Characteristics of activation of cathepsin B by sodium salicylate and comparison of catalytic site properties of cathepsin B and H. Jpn. J. Pharmacol 39, 207-215
    • (1985) Jpn. J. Pharmacol , vol.39 , pp. 207-215
    • Yamamoto, K.1    Takeda, M.2    Kato, Y.3
  • 14
    • 0022742338 scopus 로고
    • Purification and tissue distribution of rat cathepsin L.
    • Bando, Y., Kominami, E., and Katunuma, N. (1986) Purification and tissue distribution of rat cathepsin L. J. Biochem. 100, 35 42
    • (1986) J. Biochem. , vol.100 , pp. 35-42
    • Bando, Y.1    Kominami, E.2    Katunuma, N.3
  • 15
    • 0027965730 scopus 로고
    • Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodental disease from the culture supernatant of Porphyromonas gingivalis
    • Kadowaki, T., Yoneda, M., Okamoto, K., Maeda, K., and Yamamoto, K. (1994) Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodental disease from the culture supernatant of Porphyromonas gingivalis. J. Biol. Chem. 269, 21371 21378
    • (1994) J. Biol. Chem. , vol.269 , pp. 21371-21378
    • Kadowaki, T.1    Yoneda, M.2    Okamoto, K.3    Maeda, K.4    Yamamoto, K.5
  • 16
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and Jagow, G.V. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368 379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Jagow, G.V.2
  • 17
    • 0001400357 scopus 로고
    • Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH gradients
    • Svensson, H. (1962) Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH gradients. Acta Chem. Scand. 16, 456-466
    • (1962) Acta Chem. Scand. , vol.16 , pp. 456-466
    • Svensson, H.1
  • 18
    • 0021672206 scopus 로고
    • L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide, a chromogenic substrate for thiol proteinase assay
    • Filippova, I.Y., Lysogorskaya, E.N., Oksenoit, E.S., Rudenskaya, G.N., and Stephanov, V.M. (1984) L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide, a chromogenic substrate for thiol proteinase 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    Stephanov, V.M.5
  • 19
    • 0009704509 scopus 로고
    • Evidence for nonidentical chains in the β-galactosidase of Escherichia coli K12
    • Steers, E., Craven, G.R., Jr., Anfinsen, C.B., and Bethune, J.L. (1965) Evidence for nonidentical chains in the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 240, 2478 2484
    • (1965) J. Biol. Chem. , vol.240 , pp. 2478-2484
    • Steers, E.1    Craven Jr., G.R.2    Anfinsen, C.B.3    Bethune, J.L.4
  • 21
    • 0021312893 scopus 로고
    • Amino acid analysis by reverse-phase high performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate
    • Heinrikson, R.L. and Meredith, S.C. (1984) Amino acid analysis by reverse-phase high performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate. Anal. Biochem. 136, 65-74
    • (1984) Anal. Biochem. , vol.136 , pp. 65-74
    • Heinrikson, R.L.1    Meredith, S.C.2
  • 22
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxy-methylated proteins
    • Crestifield, A.M., Moore, S., and Stein, W.H. (1963) The preparation and enzymatic hydrolysis of reduced and S-carboxy-methylated proteins. J. Biol. Chem. 238, 622-627
    • (1963) J. Biol. Chem. , vol.238 , pp. 622-627
    • Crestifield, A.M.1    Moore, S.2    Stein, W.H.3
  • 23
    • 0024066065 scopus 로고
    • The 2.0 a X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W., Enbh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J., and Turk, V. (1988) The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7, 2593 2599
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Enbh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 24
    • 0001612653 scopus 로고
    • Vacuolar processing enzyme responsible for maturation of seed proteins
    • Hara-Nishimura, I., Shimada, T., Hiraiwa, N., and Nishimura, M. (1995) Vacuolar processing enzyme responsible for maturation of seed proteins. J. Plant Physiol. 145, 632 640
    • (1995) J. Plant Physiol. , vol.145 , pp. 632-640
    • Hara-Nishimura, I.1    Shimada, T.2    Hiraiwa, N.3    Nishimura, M.4
  • 25
    • 0022385232 scopus 로고
    • Amino acid sequence of derivatives of newborn rat epidermal thiol proteinase inhibitor
    • Takeda, A., Kaji, H., Nakaya, K., Aoki, Y., Nakamura, Y., and Samejima, T. (1985) Amino acid sequence of derivatives of newborn rat epidermal thiol proteinase inhibitor. Biochem. Int. 11, 557 564
    • (1985) Biochem. Int. , vol.11 , pp. 557-564
    • Takeda, A.1    Kaji, H.2    Nakaya, K.3    Aoki, Y.4    Nakamura, Y.5    Samejima, T.6
  • 26
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors, human cystatin C and chicken cystatin
    • Abrahamson, M., Ritonja, A., Brown, M.A., Grubb, A., Machleidt, W., and Barrett, A.J. (1987) Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors, human cystatin C and chicken cystatin. J. Biol. Chem. 262, 9688 9694
    • (1987) J. Biol. Chem. , vol.262 , pp. 9688-9694
    • Abrahamson, M.1    Ritonja, A.2    Brown, M.A.3    Grubb, A.4    Machleidt, W.5    Barrett, A.J.6
  • 28
    • 0024278653 scopus 로고
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. J. Biol. Chem. 263, 7655-7659
    • (1988) J. Biol. Chem. , vol.263 , pp. 7655-7659
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Arai, S.4    Suzuki, K.5
  • 29
    • 0025047273 scopus 로고
    • N-terminal variants of recombinant stefin B: Effect on affinity for papain and cathepsin B
    • Thiele, U., Assfalg-Machleidt, I., Machleidt, W., and Auerswald, E.A. (1990) N-terminal variants of recombinant stefin B: Effect on affinity for papain and cathepsin B. Biol. Chem. Hoppe-Seyler 371, Suppl., 125-136
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , Issue.SUPPL. , pp. 125-136
    • Thiele, U.1    Assfalg-Machleidt, I.2    Machleidt, W.3    Auerswald, E.A.4
  • 30
    • 0026215090 scopus 로고
    • Some properties of a cysteine proteinase inhibitor from corn endosperm
    • Abe, M. and Arai, S. (1991) Some properties of a cysteine proteinase inhibitor from corn endosperm. Agric. Biol. Chem. 55, 2417 2418
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2417-2418
    • Abe, M.1    Arai, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.