메뉴 건너뛰기




Volumn 3, Issue 3, 2009, Pages 175-184

Protease analysis by zymography: A review on techniques and patents

Author keywords

Electrophoresis; Enzymes; In situ zymography; Matrix metallo proteases; Multiple layer zymography; Proteases; Two dimensional zymography

Indexed keywords

ENZYME ACTIVITY; MOLECULAR BIOLOGY; PATENTS AND INVENTIONS;

EID: 70449108908     PISSN: 18722083     EISSN: None     Source Type: Journal    
DOI: 10.2174/187220809789389162     Document Type: Review
Times cited : (39)

References (88)
  • 1
    • 0028334115 scopus 로고
    • Zymographic techniques for detection and characterization of microbial proteases
    • Lantz MS, Ciborowski P. Zymographic techniques for detection and characterization of microbial proteases. Methods Enzymol 1994; 235: 563-594.
    • (1994) Methods Enzymol , vol.235 , pp. 563-594
    • Lantz, M.S.1    Ciborowski, P.2
  • 3
    • 0031570725 scopus 로고    scopus 로고
    • Zymography: A single-step staining method for quantitation of proteolytic activity on substrate gels
    • Leber TM, Balkwill FR. Zymography: A single-step staining method for quantitation of proteolytic activity on substrate gels. Anal Biochem 1997; 249: 24-28.
    • (1997) Anal Biochem , vol.249 , pp. 24-28
    • Leber, T.M.1    Balkwill, F.R.2
  • 4
    • 12344258657 scopus 로고    scopus 로고
    • Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors
    • Snoek-van Beurden PA, Von den Hoff JW. Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors. Biotechniques 2005; 38: 73-83.
    • (2005) Biotechniques , vol.38 , pp. 73-83
    • Snoek-van Beurden, P.A.1    Von den Hoff, J.W.2
  • 5
    • 0001362081 scopus 로고
    • Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels
    • Hunter RL, Markert CL. Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels. Science 1957; 125: 1294-1295.
    • (1957) Science , vol.125 , pp. 1294-1295
    • Hunter, R.L.1    Markert, C.L.2
  • 6
    • 0001508463 scopus 로고
    • The relationship between fixation and techniques for the histochemical localization of hydrolytic enzymes
    • Burstone MS. The relationship between fixation and techniques for the histochemical localization of hydrolytic enzymes. J Histochem Cytochem 1958; 6: 322-339.
    • (1958) J Histochem Cytochem , vol.6 , pp. 322-339
    • Burstone, M.S.1
  • 7
    • 0345691033 scopus 로고
    • The distribution of esterases in mouse tissues
    • Markert CL, Hunter RL. The distribution of esterases in mouse tissues. J Histochem Cytochem 1959; 7: 42-49.
    • (1959) J Histochem Cytochem , vol.7 , pp. 42-49
    • Markert, C.L.1    Hunter, R.L.2
  • 8
    • 0000535586 scopus 로고
    • Multiple forms of enzymes: Tissue, ontogenetic, and species specific patterns
    • Markert CL, Moller F. Multiple forms of enzymes: Tissue, ontogenetic, and species specific patterns. Proc Natl Acad Sci USA 1959; 45: 753-763.
    • (1959) Proc Natl Acad Sci USA , vol.45 , pp. 753-763
    • Markert, C.L.1    Moller, F.2
  • 9
    • 70449135444 scopus 로고
    • A histochemical study of enzymes in the epididymis of normal, castrated and hormone replaced castrated mice separated by zone electrophoresis in starch gels
    • Allen JM, Hunter RL. A histochemical study of enzymes in the epididymis of normal, castrated and hormone replaced castrated mice separated by zone electrophoresis in starch gels. J Histochem Cytochem 1960; 8: 50-57.
    • (1960) J Histochem Cytochem , vol.8 , pp. 50-57
    • Allen, J.M.1    Hunter, R.L.2
  • 10
    • 27144493006 scopus 로고
    • The zymogram as a tool for the characterization of enzyme substrate specificity
    • Hunter RL, Burstone MS. The zymogram as a tool for the characterization of enzyme substrate specificity. J Histochem Cytochem 1960; 8: 58-62.
    • (1960) J Histochem Cytochem , vol.8 , pp. 58-62
    • Hunter, R.L.1    Burstone, M.S.2
  • 11
    • 0000882492 scopus 로고
    • Genetic studies on mutant enzymes in maize: Synthesis of hybrid enzymes by heterozygotes
    • Schwartz D. Genetic studies on mutant enzymes in maize: Synthesis of hybrid enzymes by heterozygotes. Proc Natl Acad Sci USA 1960; 46: 1210-1215.
    • (1960) Proc Natl Acad Sci USA , vol.46 , pp. 1210-1215
    • Schwartz, D.1
  • 12
    • 70449120711 scopus 로고
    • Serum esterases in mice, rats and man using the two-dimensional zymogram method
    • Hunter RL, Denuce JM, Strachan DS. Serum esterases in mice, rats and man using the two-dimensional zymogram method. Ann Histochim 1961; 6: 447-455.
    • (1961) Ann Histochim , vol.6 , pp. 447-455
    • Hunter, R.L.1    Denuce, J.M.2    Strachan, D.S.3
  • 13
    • 0014360039 scopus 로고
    • Chromosomes of the zebra fish: A model for cytogenetic, embryologic, and ecologic study
    • Endo A, Ingalls TH. Chromosomes of the zebra fish: A model for cytogenetic, embryologic, and ecologic study. J Hered 1968; 59: 382-384.
    • (1968) J Hered , vol.59 , pp. 382-384
    • Endo, A.1    Ingalls, T.H.2
  • 14
    • 84960595215 scopus 로고
    • Key lectureship announced
    • Wilhelmine E. Key lectureship announced. J Hered 1964; 55: 285.
    • (1964) J Hered , vol.55 , pp. 285
    • Wilhelmine, E.1
  • 15
    • 0015028254 scopus 로고
    • Molecular heterogeneity of human serum cholinesterase
    • LaMotta RV, Woronick CL. Molecular heterogeneity of human serum cholinesterase. Clin Chem 1971; 17: 135-144.
    • (1971) Clin Chem , vol.17 , pp. 135-144
    • LaMotta, R.V.1    Woronick, C.L.2
  • 16
    • 0018841102 scopus 로고
    • Acid phosphatase in Gaucher's disease
    • Robinson DB, Glew RH. Acid phosphatase in Gaucher's disease. Clin Chem 1980; 26: 371-382.
    • (1980) Clin Chem , vol.26 , pp. 371-382
    • Robinson, D.B.1    Glew, R.H.2
  • 18
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C, Dowdle EB. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal Biochem 1980; 102: 196-202.
    • (1980) Anal Biochem , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 20
    • 0025647386 scopus 로고
    • Purification and characterization of extracellular matrix-degrading metalloproteinase, Matrin (Pump-1), secreted from human rectal carcinoma cell line
    • Miyazaki K, Hattori Y, Umenishi F, Yasumitsu H, Umeda M. Purification and characterization of extracellular matrix-degrading metalloproteinase, Matrin (Pump-1), secreted from human rectal carcinoma cell line. Cancer Res 1990; 50: 7758-7764.
    • (1990) Cancer Res , vol.50 , pp. 7758-7764
    • Miyazaki, K.1    Hattori, Y.2    Umenishi, F.3    Yasumitsu, H.4    Umeda, M.5
  • 22
    • 0031767816 scopus 로고    scopus 로고
    • Staphylococcal cell wall: Morphogenesis and fatal variations in the presence of penicillin
    • Giesbrecht P, Kersten T, Maidhof H, Wecke J. Staphylococcal cell wall: Morphogenesis and fatal variations in the presence of penicillin. Microbiol Mol Biol Rev 1998; 62: 1371-1414.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1371-1414
    • Giesbrecht, P.1    Kersten, T.2    Maidhof, H.3    Wecke, J.4
  • 23
    • 0041523879 scopus 로고    scopus 로고
    • Expanding the use of zymography by the chemical linkage of small, defined substrates to the gel matrix
    • Kaberdin VR, McDowall KJ. Expanding the use of zymography by the chemical linkage of small, defined substrates to the gel matrix. Genome Res 2003; 13: 1961-1965.
    • (2003) Genome Res , vol.13 , pp. 1961-1965
    • Kaberdin, V.R.1    McDowall, K.J.2
  • 24
    • 2542569423 scopus 로고    scopus 로고
    • Metabolic mapping of proteinase activity with emphasis on in situ zymography of gelatinases: Review and protocols
    • Frederiks WM, Mook ORF. Metabolic mapping of proteinase activity with emphasis on in situ zymography of gelatinases: Review and protocols. J Histochem Cytochem 2004; 52: 711-722.
    • (2004) J Histochem Cytochem , vol.52 , pp. 711-722
    • Frederiks, W.M.1    Mook, O.R.F.2
  • 25
    • 0032526292 scopus 로고    scopus 로고
    • The detection of enzyme activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Bischoff KM, Shi L, Kennelly PJ. The detection of enzyme activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem 1998; 260: 1-17.
    • (1998) Anal Biochem , vol.260 , pp. 1-17
    • Bischoff, K.M.1    Shi, L.2    Kennelly, P.J.3
  • 26
    • 0001571153 scopus 로고
    • The diversity of proteolytic enzymes
    • Beynon RJ, Bond JS, Eds. IRL Press at Oxford University Press: Oxford
    • Neurath H. The diversity of proteolytic enzymes. Proteolytic Enzymes: a practical approach. In: Beynon RJ, Bond JS, Eds. IRL Press at Oxford University Press: Oxford 1989; 1-13.
    • (1989) Proteolytic Enzymes: A practical approach , pp. 1-13
    • Neurath, H.1
  • 27
    • 0032426798 scopus 로고    scopus 로고
    • Intracellular proteinases of invertebrates: Calcium-dependent and proteasome/ubiquitin-dependent systems
    • Mykles DL. Intracellular proteinases of invertebrates: Calcium-dependent and proteasome/ubiquitin-dependent systems. Int Rev Cytol 1998; 184: 157-289.
    • (1998) Int Rev Cytol , vol.184 , pp. 157-289
    • Mykles, D.L.1
  • 28
    • 0028673152 scopus 로고
    • Classification of peptidases
    • Barret AJ. Classification of peptidases. Methods Enzymol 1994; 244: 1-15.
    • (1994) Methods Enzymol , vol.244 , pp. 1-15
    • Barret, A.J.1
  • 29
    • 0027485558 scopus 로고
    • Substrate-Gel Electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinases inhibitors
    • García-Carreño FL, Dimes LE, Haard NF. Substrate-Gel Electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinases inhibitors. Anal Biochem 1993; 214: 65-69.
    • (1993) Anal Biochem , vol.214 , pp. 65-69
    • García-Carreño, F.L.1    Dimes, L.E.2    Haard, N.F.3
  • 30
    • 0000248904 scopus 로고    scopus 로고
    • Structure and function of serine proteases
    • Neuberger A, Brocklehurst K, Eds. Elsevier Science Publishers B. V
    • Polgár L. Structure and function of serine proteases. Hydrolytic enzymes. In: Neuberger A, Brocklehurst K, Eds. Elsevier Science Publishers B. V., 1987; 159-163.
    • Hydrolytic enzymes , vol.1987 , pp. 159-163
    • Polgár, L.1
  • 32
    • 0002038716 scopus 로고    scopus 로고
    • Aspartyl proteinases
    • Neuberger A, Brocklehurst K, Eds. Elsevier Science Publishers B. V
    • Fruton JS. Aspartyl proteinases. Hydrolytic Enzymes. In: Neuberger A, Brocklehurst K, Eds. Elsevier Science Publishers B. V., 1987; 1-5.
    • Hydrolytic Enzymes , vol.1987 , pp. 1-5
    • Fruton, J.S.1
  • 34
    • 85189263923 scopus 로고    scopus 로고
    • Oliver GW, Stetler WG, Kleiner DE. Zymography, Casein zymography and reverse zymography: activity assay for proteases and their inhibitors. Proteolytic enzymes, tools and targets. In: Sterchi EE, Stöcker W, Eds. Springer Verlag: Berlin 1999; 63-76.
    • Oliver GW, Stetler WG, Kleiner DE. Zymography, Casein zymography and reverse zymography: activity assay for proteases and their inhibitors. Proteolytic enzymes, tools and targets. In: Sterchi EE, Stöcker W, Eds. Springer Verlag: Berlin 1999; 63-76.
  • 35
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteases: Structures, evolution and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S. Matrix metalloproteases: Structures, evolution and diversification. FASEB J 1998; 12: 1075-1095.
    • (1998) FASEB J , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 36
    • 0034752257 scopus 로고    scopus 로고
    • Zymographic analysis of circulating and tissue forms of colon carcinoma gelatinase A (MMP-2) and B (MMP-9) separated by mono- and two-dimensional electrophoresis
    • Pucci-Minafra I, Minafra S, La Rocca G, et al. Zymographic analysis of circulating and tissue forms of colon carcinoma gelatinase A (MMP-2) and B (MMP-9) separated by mono- and two-dimensional electrophoresis. Matrix Biol 2001; 20: 419-427.
    • (2001) Matrix Biol , vol.20 , pp. 419-427
    • Pucci-Minafra, I.1    Minafra, S.2    La Rocca, G.3
  • 37
    • 85189262024 scopus 로고    scopus 로고
    • Konno, K., Umezawa, E.: WO2006041130 (2006).
    • Konno, K., Umezawa, E.: WO2006041130 (2006).
  • 41
    • 85189279837 scopus 로고    scopus 로고
    • Tesfaigzi, Y., Belinsky, S.: WO2005017113 (2005).
    • Tesfaigzi, Y., Belinsky, S.: WO2005017113 (2005).
  • 42
    • 85189274794 scopus 로고    scopus 로고
    • Moses, M., Yan, L.: EP1832876 (2007).
    • Moses, M., Yan, L.: EP1832876 (2007).
  • 43
    • 85189276044 scopus 로고    scopus 로고
    • Golubnitschaja, O., Holz, F.: EP1865071 (2007).
    • Golubnitschaja, O., Holz, F.: EP1865071 (2007).
  • 44
    • 85189267652 scopus 로고    scopus 로고
    • Jenkin, G., Trounson, A., Wallace, E., Moodley, Y., Manuelpillai, U., Ilancheran, S.: WO2008144820 (2008).
    • Jenkin, G., Trounson, A., Wallace, E., Moodley, Y., Manuelpillai, U., Ilancheran, S.: WO2008144820 (2008).
  • 45
    • 85189258588 scopus 로고    scopus 로고
    • Kopf, M., Romani, L., Kastelein, R., Chackerian, A.: WO2008153610 (2008).
    • Kopf, M., Romani, L., Kastelein, R., Chackerian, A.: WO2008153610 (2008).
  • 46
    • 85189260640 scopus 로고    scopus 로고
    • Pirilä, E., Suojanen, J., Sorsa, T., Salo, T., Koivunen, E.: WO2009000971 (2009).
    • Pirilä, E., Suojanen, J., Sorsa, T., Salo, T., Koivunen, E.: WO2009000971 (2009).
  • 47
    • 85189269769 scopus 로고    scopus 로고
    • Dubin, G., Potempa, J.: WO2008153429 (2008).
    • Dubin, G., Potempa, J.: WO2008153429 (2008).
  • 48
    • 0000827238 scopus 로고
    • Detection, quantification, and characterization of proteases in recombinant Escherichia coli
    • Harcum S, Bentley WE. Detection, quantification, and characterization of proteases in recombinant Escherichia coli. Biotechnol Tech 1993; 7: 441-447.
    • (1993) Biotechnol Tech , vol.7 , pp. 441-447
    • Harcum, S.1    Bentley, W.E.2
  • 49
    • 0028345645 scopus 로고
    • Quantitative zymography: Detection of picogram quantities of gelatinases
    • Kleiner DE, Stetler-S WG. Quantitative zymography: Detection of picogram quantities of gelatinases. Anal Biochem 1994; 218: 325-329.
    • (1994) Anal Biochem , vol.218 , pp. 325-329
    • Kleiner, D.E.1    Stetler-S, W.G.2
  • 50
    • 0031570725 scopus 로고    scopus 로고
    • Zymography: A single-step staining method for quantitation of proteolytic activity on substrate gels
    • Leber TM, Balkwill FR. Zymography: A single-step staining method for quantitation of proteolytic activity on substrate gels. Anal Biochem 1997; 249: 24-28.
    • (1997) Anal Biochem , vol.249 , pp. 24-28
    • Leber, T.M.1    Balkwill, F.R.2
  • 51
    • 0032518450 scopus 로고    scopus 로고
    • Collagen zymography as a sensitive and specific technique for the determination of subpicogram levels of interstitial collagenase
    • Gogly B, Groult N, Hornebeck W, Godeau G, Pellat B. Collagen zymography as a sensitive and specific technique for the determination of subpicogram levels of interstitial collagenase. Anal Biochem 1998; 255: 211-216.
    • (1998) Anal Biochem , vol.255 , pp. 211-216
    • Gogly, B.1    Groult, N.2    Hornebeck, W.3    Godeau, G.4    Pellat, B.5
  • 52
    • 0032744354 scopus 로고    scopus 로고
    • Quantitative zymography of matrix metalloproteinases by measuring hydroxyproline: Application to gelatinases A and B
    • Lê J, Dauchot P, Perrot JL, Cambazard F, Frey J, Chamson A. Quantitative zymography of matrix metalloproteinases by measuring hydroxyproline: Application to gelatinases A and B. Electrophoresis 1999; 20: 2824-2829.
    • (1999) Electrophoresis , vol.20 , pp. 2824-2829
    • Lê, J.1    Dauchot, P.2    Perrot, J.L.3    Cambazard, F.4    Frey, J.5    Chamson, A.6
  • 53
    • 0035619638 scopus 로고    scopus 로고
    • Comparison of three substrates (casein, fibrin, and gelatin) in zymographic gel
    • Choi NS, Yoon KS, Lee JY, Han KY, Kim SH. Comparison of three substrates (casein, fibrin, and gelatin) in zymographic gel. J Biochem Mol Biol 2001; 34: 531-536.
    • (2001) J Biochem Mol Biol , vol.34 , pp. 531-536
    • Choi, N.S.1    Yoon, K.S.2    Lee, J.Y.3    Han, K.Y.4    Kim, S.H.5
  • 54
    • 38449092398 scopus 로고    scopus 로고
    • Zymography-method for quantitation of activity on gelatinase A (pro-MMP-2, 72 kDa) and gelatinase B (pro-MMP-9, 92 kDa) in serum of patients with breast cancer
    • Sliwowska I, Kopczyński Z. Zymography-method for quantitation of activity on gelatinase A (pro-MMP-2, 72 kDa) and gelatinase B (pro-MMP-9, 92 kDa) in serum of patients with breast cancer. Wiad Lek 2007; 60: 241-247.
    • (2007) Wiad Lek , vol.60 , pp. 241-247
    • Sliwowska, I.1    Kopczyński, Z.2
  • 55
    • 85189257815 scopus 로고    scopus 로고
    • Invitrogen Life Science Catalog. Chapter 22 Electrophoresis. Novex® Zymogram Gels. 2005; pp. 437-440. [Date of access June/07/2009]. http://www.invitrogen.com/etc/medialib/en/filelibrary/ pdf/Catalogs/2005-Life-Sciences-Catalog.Par.61111.File.dat/ Chapter22.pdf
    • Invitrogen Life Science Catalog. Chapter 22 Electrophoresis. "Novex® Zymogram Gels." 2005; pp. 437-440. [Date of access June/07/2009]. http://www.invitrogen.com/etc/medialib/en/filelibrary/ pdf/Catalogs/2005-Life-Sciences-Catalog.Par.61111.File.dat/ Chapter22.pdf
  • 56
    • 0036850364 scopus 로고    scopus 로고
    • Gelatin zymography and substrate cleavage assays of matrix metalloproteinase-2 in breast carcinoma cells overexpressing membrane type-1 matrix metalloproteinase
    • Ratnoikov BI, Deryugina EI, Strongin AY. Gelatin zymography and substrate cleavage assays of matrix metalloproteinase-2 in breast carcinoma cells overexpressing membrane type-1 matrix metalloproteinase. Lab Invest 2002; 82: 1583-1590.
    • (2002) Lab Invest , vol.82 , pp. 1583-1590
    • Ratnoikov, B.I.1    Deryugina, E.I.2    Strongin, A.Y.3
  • 58
    • 85189279168 scopus 로고    scopus 로고
    • US20090004302
    • Cyr, B.: US20090004302 (2009).
    • (2009)
    • Cyr, B.1
  • 59
  • 60
    • 0030977362 scopus 로고    scopus 로고
    • Analysis of proteins from different phase variants of the entomopathogenic bacteria Photorhabdus luminescens by two-dimensional zymography
    • Ong KL, Chang FN. Analysis of proteins from different phase variants of the entomopathogenic bacteria Photorhabdus luminescens by two-dimensional zymography. Electrophoresis 1997; 18: 834-839.
    • (1997) Electrophoresis , vol.18 , pp. 834-839
    • Ong, K.L.1    Chang, F.N.2
  • 61
    • 0031807347 scopus 로고    scopus 로고
    • Two-dimensional zymography for analysis of proteolytic enzymes in human pure pancreatic juice
    • Kaino S, Furui T, Hatano S, Kaino M, Okita K, Nakamura K. Two-dimensional zymography for analysis of proteolytic enzymes in human pure pancreatic juice. Electrophoresis 1998; 19: 782-787.
    • (1998) Electrophoresis , vol.19 , pp. 782-787
    • Kaino, S.1    Furui, T.2    Hatano, S.3    Kaino, M.4    Okita, K.5    Nakamura, K.6
  • 62
    • 0036209257 scopus 로고    scopus 로고
    • A functional proteomic analysis of secreted fibrinolytic enzymes from Bacillus subtilis 168 using a combined method of two-dimensional gel electrophoresis and zymography
    • Park SG, Kho CW, Cho S, Lee DH, Kim SH, Park BC. A functional proteomic analysis of secreted fibrinolytic enzymes from Bacillus subtilis 168 using a combined method of two-dimensional gel electrophoresis and zymography. Proteomics 2002; 2: 206-211.
    • (2002) Proteomics , vol.2 , pp. 206-211
    • Park, S.G.1    Kho, C.W.2    Cho, S.3    Lee, D.H.4    Kim, S.H.5    Park, B.C.6
  • 63
    • 3142783406 scopus 로고    scopus 로고
    • Nano-scale proteomics approach using two-dimensional fibrin zymography combined with fluorescent SYPRO ruby dye
    • Choi NS, Yoo KH, Yoon KS, Maeng PJ, Kim SH. Nano-scale proteomics approach using two-dimensional fibrin zymography combined with fluorescent SYPRO ruby dye. J Biochem Mol Biol 2004; 37: 298-303.
    • (2004) J Biochem Mol Biol , vol.37 , pp. 298-303
    • Choi, N.S.1    Yoo, K.H.2    Yoon, K.S.3    Maeng, P.J.4    Kim, S.H.5
  • 64
    • 33846997925 scopus 로고    scopus 로고
    • Analysis of serine proteases from marine sponges by 2-D zymography
    • Wilkesman J, Schröder HC. Analysis of serine proteases from marine sponges by 2-D zymography. Electrophoresis 2007; 28: 429-436.
    • (2007) Electrophoresis , vol.28 , pp. 429-436
    • Wilkesman, J.1    Schröder, H.C.2
  • 65
    • 40849147107 scopus 로고    scopus 로고
    • One- and two-dimensional SDS-PAGE zymography with quenched fluorogenic substrates provides identification of biological fluid proteases by direct mass spectrometry
    • Thimon V, Belghazi M, Labas V, Dacheux JL, Gatti JL. One- and two-dimensional SDS-PAGE zymography with quenched fluorogenic substrates provides identification of biological fluid proteases by direct mass spectrometry. Anal Biochem 2008; 375: 382-384.
    • (2008) Anal Biochem , vol.375 , pp. 382-384
    • Thimon, V.1    Belghazi, M.2    Labas, V.3    Dacheux, J.L.4    Gatti, J.L.5
  • 66
    • 4644295009 scopus 로고    scopus 로고
    • Detection of TIMP-2-like protein in Atlantic cod (Gadus morhua) muscle using two-dimensional real-time reverse zymography
    • Lodemel JB, Egge-Jacobsen W, Olsen RL. Detection of TIMP-2-like protein in Atlantic cod (Gadus morhua) muscle using two-dimensional real-time reverse zymography. Comp Biochem Physiol B Biochem Mol Biol 2004; 139: 253-9.
    • (2004) Comp Biochem Physiol B Biochem Mol Biol , vol.139 , pp. 253-259
    • Lodemel, J.B.1    Egge-Jacobsen, W.2    Olsen, R.L.3
  • 67
    • 0036467706 scopus 로고    scopus 로고
    • Real-time zymography and reverse zymography: A method for detecting activities of matrix metalloproteinases and their inhibitors using FITC-labeled collagen and casein as substrates
    • Hattori S, Fujisaki H, Kiriyama T, Yokoyama T, Irie S. Real-time zymography and reverse zymography: A method for detecting activities of matrix metalloproteinases and their inhibitors using FITC-labeled collagen and casein as substrates. Anal Biochem 2002, 301: 27-34.
    • (2002) Anal Biochem , vol.301 , pp. 27-34
    • Hattori, S.1    Fujisaki, H.2    Kiriyama, T.3    Yokoyama, T.4    Irie, S.5
  • 69
    • 85189271969 scopus 로고    scopus 로고
    • Te, K., Johannes, M., Beekman, B.: WO97025437 (1997).
    • Te, K., Johannes, M., Beekman, B.: WO97025437 (1997).
  • 71
    • 34748866570 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins
    • Braun RJ, Kinkl N, Beer M, Ueffing M. Two-dimensional electrophoresis of membrane proteins. Anal Bioanal Chem 2007; 389: 1033-1045.
    • (2007) Anal Bioanal Chem , vol.389 , pp. 1033-1045
    • Braun, R.J.1    Kinkl, N.2    Beer, M.3    Ueffing, M.4
  • 72
    • 38449106926 scopus 로고    scopus 로고
    • Two-dimensional BAC/SDS-PAGE for membrane proteomics
    • Zahedi RP, Moebius J, Sickmann A. Two-dimensional BAC/SDS-PAGE for membrane proteomics. Subcell Biochem 2007; 43: 13-20.
    • (2007) Subcell Biochem , vol.43 , pp. 13-20
    • Zahedi, R.P.1    Moebius, J.2    Sickmann, A.3
  • 73
    • 0141591823 scopus 로고    scopus 로고
    • A review of in situ zymography: Method for localization of protease activities in a tissue
    • Nemori R, Tachikawa T. A review of in situ zymography: Method for localization of protease activities in a tissue. Tissue Culture Eng 1999; 25: 29-32.
    • (1999) Tissue Culture Eng , vol.25 , pp. 29-32
    • Nemori, R.1    Tachikawa, T.2
  • 74
    • 0038148278 scopus 로고    scopus 로고
    • In situ zymography: A molecular pathology technique to localize endogenous protease activity in tissue sections
    • Yan SJ, Blomme EA. In situ zymography: A molecular pathology technique to localize endogenous protease activity in tissue sections. Vet Pathol 2003; 40: 227-236.
    • (2003) Vet Pathol , vol.40 , pp. 227-236
    • Yan, S.J.1    Blomme, E.A.2
  • 77
    • 85189275531 scopus 로고    scopus 로고
    • Sagi, I., Danon, T., Sela, N., Shanzer, A., Arad-yellin, R., Kikkeri, R.: WO2008102359 (2008).
    • Sagi, I., Danon, T., Sela, N., Shanzer, A., Arad-yellin, R., Kikkeri, R.: WO2008102359 (2008).
  • 78
    • 0037274541 scopus 로고    scopus 로고
    • Detections of matrix metalloproteinases activities and localization by film in situ zymography (FIZ)
    • Muramatsu M, Takai S, Miyazaki M. Detections of matrix metalloproteinases activities and localization by film in situ zymography (FIZ). Nippon Yakurigaku Zasshi 2003; 121: 113-118.
    • (2003) Nippon Yakurigaku Zasshi , vol.121 , pp. 113-118
    • Muramatsu, M.1    Takai, S.2    Miyazaki, M.3
  • 79
    • 85189255941 scopus 로고    scopus 로고
    • Toshiharu, H., Shinkichi, I.: JP2002223792 (2002).
    • Toshiharu, H., Shinkichi, I.: JP2002223792 (2002).
  • 81
    • 58349096674 scopus 로고    scopus 로고
    • Multiple-layer substrate zymography for detection of several enzymes in a single sodium dodecyl sulfate gel
    • Choi NS, Kim B, Park CS, et al. Multiple-layer substrate zymography for detection of several enzymes in a single sodium dodecyl sulfate gel. Anal Biochem 2009; 386: 121-122.
    • (2009) Anal Biochem , vol.386 , pp. 121-122
    • Choi, N.S.1    Kim, B.2    Park, C.S.3
  • 82
    • 69449094890 scopus 로고    scopus 로고
    • Mixed-substrate (glycerol tributyrate and fibrin) zymography for simultaneous detection of lipolytic and proteolytic enzymes on a single gel
    • Choi NS, Choi JH, Kim, BH, et al. Mixed-substrate (glycerol tributyrate and fibrin) zymography for simultaneous detection of lipolytic and proteolytic enzymes on a single gel. Electrophoresis 2009; 30: 2234-2237.
    • (2009) Electrophoresis , vol.30 , pp. 2234-2237
    • Choi, N.S.1    Choi, J.H.2    Kim, B.H.3
  • 83
    • 41349102142 scopus 로고    scopus 로고
    • A preliminary analysis of microbial and biochemical properties of high-temperature compost
    • Oshima T, Moriya T. A preliminary analysis of microbial and biochemical properties of high-temperature compost. Ann N Y Acad Sci 2008; 1125: 338-344.
    • (2008) Ann N Y Acad Sci , vol.1125 , pp. 338-344
    • Oshima, T.1    Moriya, T.2
  • 84
    • 0036690546 scopus 로고    scopus 로고
    • Thermophilic protease-producing Geobacillus from Buranga hot springs in Western Uganda
    • Hawumba J, Theron J, Brözel V. Thermophilic protease-producing Geobacillus from Buranga hot springs in Western Uganda. Curr Microbiol 2002; 45: 144-150.
    • (2002) Curr Microbiol , vol.45 , pp. 144-150
    • Hawumba, J.1    Theron, J.2    Brözel, V.3
  • 85
    • 36849036714 scopus 로고    scopus 로고
    • Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE
    • Xia K, Maning M, Hesham H, Lin Q, Bystroff C, Colon W. Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE. Proc Natl Acad Sci USA 2007; 104: 17329-17334.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 17329-17334
    • Xia, K.1    Maning, M.2    Hesham, H.3    Lin, Q.4    Bystroff, C.5    Colon, W.6
  • 86
    • 0035486724 scopus 로고    scopus 로고
    • Assessing the diversity of marine bacterial beta-glucosidases by capillary electrophoresis zymography
    • Arrieta JM, Herndl GJ. Assessing the diversity of marine bacterial beta-glucosidases by capillary electrophoresis zymography. Appl Environ Microbiol 2001; 67: 4896-4900.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4896-4900
    • Arrieta, J.M.1    Herndl, G.J.2
  • 87
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Görg A, Weiss W, Dunn MJ. Current two-dimensional electrophoresis technology for proteomics. Proteomics 2004; 4: 3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Görg, A.1    Weiss, W.2    Dunn, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.