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Volumn 64, Issue 3, 2005, Pages 182-188

Rapid qualitative protease microassay (RPM)

Author keywords

HPLC fractions; Protease; Rapid qualitative protease microassay

Indexed keywords

ANAZOLENE SODIUM; BRILLIANT BLUE; CYSTEINE; PAPAIN; PROTEINASE;

EID: 25844453963     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbbm.2005.07.002     Document Type: Article
Times cited : (1)

References (14)
  • 1
    • 0029347066 scopus 로고
    • Association of a 33-kD cysteine protease found in maize callus with the inhibition of fall armyworm larval growth
    • B.H. Jiang, U. Siregar, K.O. Willeford, D.S. Luthe, and W.P. Williams Association of a 33-kD cysteine protease found in maize callus with the inhibition of fall armyworm larval growth Plant Physiol 108 1995 1631 1640
    • (1995) Plant Physiol , vol.108 , pp. 1631-1640
    • Jiang, B.H.1    Siregar, U.2    Willeford, K.O.3    Luthe, D.S.4    Williams, W.P.5
  • 2
    • 0033868878 scopus 로고    scopus 로고
    • A unique 33-kD cysteine proteinase accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other Lepidoptera
    • T. Pechan, L. Ye, Y.M. Chang, A. Mitra, L. Lin, and F.M. Davis A unique 33-kD cysteine proteinase accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other Lepidoptera Plant Cell 12 2000 1031 1040
    • (2000) Plant Cell , vol.12 , pp. 1031-1040
    • Pechan, T.1    Ye, L.2    Chang, Y.M.3    Mitra, A.4    Lin, L.5    Davis, F.M.6
  • 3
    • 0036790854 scopus 로고    scopus 로고
    • Insect feeding mobilizes a unique plant defense protease that disrupts the peritrophic matrix of caterpillars
    • T. Pechan, A. Cohen, W.P. Williams, and D.S. Luthe Insect feeding mobilizes a unique plant defense protease that disrupts the peritrophic matrix of caterpillars Proc. Natl Acad Sci U S A 99 2002 13319 13323
    • (2002) Proc. Natl Acad Sci U S a , vol.99 , pp. 13319-13323
    • Pechan, T.1    Cohen, A.2    Williams, W.P.3    Luthe, D.S.4
  • 4
    • 1442313959 scopus 로고    scopus 로고
    • Heterologous expression of maize Mir1 cysteine proteinase in eukaryotic and prokaryotic expression systems
    • T. Pechan, P.W.K. Ma, and D.S. Luthe Heterologous expression of maize Mir1 cysteine proteinase in eukaryotic and prokaryotic expression systems Protein Expr Purif 34 2004 134 141
    • (2004) Protein Expr Purif , vol.34 , pp. 134-141
    • Pechan, T.1    Ma, P.W.K.2    Luthe, D.S.3
  • 5
    • 0017219081 scopus 로고
    • Acidic cysteine protease inhibitors from pineapple stems
    • R.L. Heinrikson, and F.J. Kezdy Acidic cysteine protease inhibitors from pineapple stems Methods Enzymol 65 1976 740 751
    • (1976) Methods Enzymol , vol.65 , pp. 740-751
    • Heinrikson, R.L.1    Kezdy, F.J.2
  • 6
    • 0019891335 scopus 로고
    • Rapid interaction of cathepsin L by Z-Phe-PheCHN12 and Z-Phe-AlaCHN2
    • H. Kirschke, and E. Shaw Rapid interaction of cathepsin L by Z-Phe-PheCHN12 and Z-Phe-AlaCHN2 Biochem Biophys Res Commun 101 1981 454 455
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 454-455
    • Kirschke, H.1    Shaw, E.2
  • 7
    • 0025959153 scopus 로고
    • Photometric or fluorometric assay of cathepsin B, L and H and papain using substrates with an aminotrifluoromethylcoumarin leaving group
    • J.R. Tchoupe, T. Moreau, F. Gauthier, and J.G. Beith Photometric or fluorometric assay of cathepsin B, L and H and papain using substrates with an aminotrifluoromethylcoumarin leaving group Biochim Biophys Acta 1076 1991 149 151
    • (1991) Biochim Biophys Acta , vol.1076 , pp. 149-151
    • Tchoupe, J.R.1    Moreau, T.2    Gauthier, F.3    Beith, J.G.4
  • 8
    • 0027458625 scopus 로고    scopus 로고
    • Electrophoretic analysis of plant cysteine and serine proteinases using gelatin-containing polyacrylamide gels and class specific proteinase inhibitors
    • Michaud D, Faye L, Yelle S. Electrophoretic analysis of plant cysteine and serine proteinases using gelatin-containing polyacrylamide gels and class specific proteinase inhibitors. Electrophoresis 14:94-8.
    • Electrophoresis , vol.14 , pp. 94-98
    • Michaud, D.1    Faye, L.2    Yelle, S.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. Bradford A rapid and sensitive method for the quantitation of 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.1
  • 11
    • 0018436661 scopus 로고
    • Maleylatioin and pH dependence of Streptomyces griseus protease B
    • S. Shinar, and A. Gertler Maleylatioin and pH dependence of Streptomyces griseus protease B Int J Pept Protein Res 13 1979 218 221
    • (1979) Int J Pept Protein Res , vol.13 , pp. 218-221
    • Shinar, S.1    Gertler, A.2
  • 12
    • 0019948262 scopus 로고
    • L-trans-epoxysuccinyl-leucylamino (4-guanidino) butane (E- 64) and its analogues and inhibitors of cysteine proteinases including cathepsins B, H, and L
    • A.J. Barrett, A.A. Kembhavi, M.A. Brown, H. Kirschke, C.G. Knight, and M. Tami l-trans-epoxysuccinyl-leucylamino (4-guanidino) butane (E- 64) and its analogues and inhibitors of cysteine proteinases including cathepsins B, H, and L Biochem J 201 1982 189 198
    • (1982) Biochem J , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tami, M.6
  • 13
    • 0031554927 scopus 로고    scopus 로고
    • Quenched BODIPY dye-labeled casein substrates for the assay of protease activity by direct fluorescence measurement
    • L.J. Jones, R.H. Upson, R.P. Haugland, N. Panchuk-Voloshina, M. Zhou, and R.P. Haugland Quenched BODIPY dye-labeled casein substrates for the assay of protease activity by direct fluorescence measurement Anal Biochem 251 1997 144 152
    • (1997) Anal Biochem , vol.251 , pp. 144-152
    • Jones, L.J.1    Upson, R.H.2    Haugland, R.P.3    Panchuk-Voloshina, N.4    Zhou, M.5    Haugland, R.P.6
  • 14
    • 0028337023 scopus 로고
    • New substrates of papain, based on the conserved sequence of natural inhibitors of the cystatin family
    • C. Serveau, L. Juliano, P. Bernard, T. Moreau, R. Mayer, and F. Gauthier New substrates of papain, based on the conserved sequence of natural inhibitors of the cystatin family Biochimie 76 1994 153 158
    • (1994) Biochimie , vol.76 , pp. 153-158
    • Serveau, C.1    Juliano, L.2    Bernard, P.3    Moreau, T.4    Mayer, R.5    Gauthier, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.