메뉴 건너뛰기




Volumn 46, Issue 8, 2011, Pages 1654-1662

Purification and biochemical characterization of a chymotrypsin-like serine protease from Euphorbia neriifolia Linn.

Author keywords

Chymotrypsin; Euphorbia neriifolia; Euphorbiaceae; Neriifolin; Serine protease

Indexed keywords

CHYMOTRYPSIN; EUPHORBIA NERIIFOLIA; EUPHORBIACEAE; NERIIFOLIN; SERINE PROTEASE;

EID: 79959919661     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.05.013     Document Type: Article
Times cited : (28)

References (46)
  • 2
    • 0012758082 scopus 로고
    • Novel enzyme combinations: A new tool to improve baking results
    • S. Haarasilta, and T. Pullinen Novel enzyme combinations: a new tool to improve baking results Agro-Food-Ind Hi-Tech 3 1992 12 13
    • (1992) Agro-Food-Ind Hi-Tech , vol.3 , pp. 12-13
    • Haarasilta, S.1    Pullinen, T.2
  • 3
    • 33745821234 scopus 로고    scopus 로고
    • Microbiology and industrial biotechnology of food-grade proteases: A perspective
    • A. Sumantha, C. Larroche, and A. Pandey Microbiology and industrial biotechnology of food grade proteases: a perspective Food Technol Biotechnol 44 2 2006 211 220 (Pubitemid 44033844)
    • (2006) Food Technology and Biotechnology , vol.44 , Issue.2 , pp. 211-220
    • Sumantha, A.1    Larroche, C.2    Pandey, A.3
  • 4
    • 0034003649 scopus 로고    scopus 로고
    • Purification and characterization of a stable cysteine protease Ervatamin B, with two disulfide bridges, from the latex of Ervatamia coronaria
    • DOI 10.1021/jf990661j
    • S. Kundu, M. Sundd, and M.V. Jagannadham Purification and characterization of a stable cysteine protease ervatamin B, with two disulfide bridges, from the latex of Ervatamia coronaria J Agric Food Chem 48 2000 171 179 (Pubitemid 30120338)
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.2 , pp. 171-179
    • Kundu, S.1    Sundd, M.2    Jagannadham, M.V.3
  • 5
    • 56449110233 scopus 로고    scopus 로고
    • A kinetically stable plant subtilase with unique peptide mass fingerprints and dimerization properties
    • DOI 10.1016/j.bpc.2008.09.019, PII S030146220800210X
    • S.C. Yadav, M.V. Jagannadham, S. Kundu, and M.V. Jagannadham A kinetically stable plant subtilase with unique peptide mass fingerprints and dimerization properties Biophys Chem 139 2009 13 23 (Pubitemid 50310060)
    • (2009) Biophysical Chemistry , vol.139 , Issue.1 , pp. 13-23
    • Yadav, S.C.1    Jagannadham, M.V.2    Kundu, S.3    Jagannadham, M.V.4
  • 6
    • 74449092835 scopus 로고    scopus 로고
    • Purification of a novel cysteine protease, procerain B, from Calotropis procera with distinct characteristics compared to procerain
    • A.N. Singh, A.K. Shukla, M.V. Jagannadham, and V.K. Dubey Purification of a novel cysteine protease, procerain B, from Calotropis procera with distinct characteristics compared to procerain Process Biochem 45 2010 399 406
    • (2010) Process Biochem , vol.45 , pp. 399-406
    • Singh, A.N.1    Shukla, A.K.2    Jagannadham, M.V.3    Dubey, V.K.4
  • 7
    • 0030068923 scopus 로고    scopus 로고
    • Protease-catalyzed incorporation of 18 O into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry
    • M. Schnölzer, P. Jedrzejewski, and W.D. Lehmann Protease-catalyzed incorporation of 18 O into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry Electrophoresis 17 5 1996 945 953
    • (1996) Electrophoresis , vol.17 , Issue.5 , pp. 945-953
    • Schnölzer, M.1    Jedrzejewski, P.2    Lehmann, W.D.3
  • 8
    • 0037010769 scopus 로고    scopus 로고
    • Purification and characterization of a hydrophobic amino acid - Specific endopeptidase from Halobacterium halobium S9 with potential application in debittering of protein hydrolysates
    • DOI 10.1016/S0032-9592(02)00180-2, PII S0032959202001802
    • H. Capiralla, T. Hiroi, T. Hirokawa, and S. Maeda Purification and characterization of hydrophobic amino acid-specific endopeptidase from Halobactrium halobium S9 with potential application in debittering of protein hydrolysates Process Biochem 38 2002 571 579 (Pubitemid 35343663)
    • (2002) Process Biochemistry , vol.38 , Issue.4 , pp. 571-579
    • Capiralla, H.1    Hiroi, T.2    Hirokawa, T.3    Maeda, S.4
  • 9
    • 40549120904 scopus 로고    scopus 로고
    • A stable serine protease, wrightin, from the latex of the plant Wrightia tinctoria (Roxb.) R. Br.: Purification and biochemical properties
    • DOI 10.1021/jf0726536
    • R. Tomar, R. Kumar, and M.V. Jagannadham A stable serine protease, wrightin, from the latex of the plant Wrightia tinctoria (Roxb.): purification and biochemical properties J Agric Food Chem 56 2008 1479 1487 (Pubitemid 351364086)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.4 , pp. 1479-1487
    • Tomar, R.1    Kumar, R.2    Jagannadham, M.V.3
  • 10
    • 24344495312 scopus 로고    scopus 로고
    • Plant serine proteases: Biochemical, physiological and molecular features
    • DOI 10.1016/j.plaphy.2005.05.001, PII S0981942805001270
    • C.M. Antao, and F.X. Malcata Plant serine proteases: biochemical, physiological and molecular features Plant Physiol Biochem 4 2005 637 650 (Pubitemid 41253443)
    • (2005) Plant Physiology and Biochemistry , vol.43 , Issue.7 , pp. 637-650
    • Antao, C.M.1    Malcata, F.X.2
  • 11
    • 78049463920 scopus 로고    scopus 로고
    • A comprehensive phyto-pharmacological review of Euphorbia neriifolia Linn
    • P. Bigoniya, and A.C. Rana A comprehensive phyto-pharmacological review of Euphorbia neriifolia Linn Pharmacogn Rev 2 4 2008 57 66
    • (2008) Pharmacogn Rev , vol.2 , Issue.4 , pp. 57-66
    • Bigoniya, P.1    Rana, A.C.2
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.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.M.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 34447632032 scopus 로고    scopus 로고
    • Carnein, a serine protease from noxious plant weed Ipomoea carnea (Morning glory)
    • DOI 10.1021/jf063700h
    • A.K. Patel, V.K. Singh, and M.V. Jagannadham Carnein, a serine protease from noxious plant weed Ipomoea carnea (morning glory) J Agric Food Chem 55 2007 5809 5818 (Pubitemid 47092962)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.14 , pp. 5809-5818
    • Patel, A.K.1    Singh, V.K.2    Jagannadham, M.V.3
  • 16
    • 0012387041 scopus 로고    scopus 로고
    • Chemical methods of analysis of glycoproteins
    • J.M. Walker, Humana Press Totawa, NJ
    • E.F. Hounsell, M.J. Davies, and K.D. Smith Chemical methods of analysis of glycoproteins J.M. Walker, The Protein Protocol Hand Book 1997 Humana Press Totawa, NJ 633 634
    • (1997) The Protein Protocol Hand Book , pp. 633-634
    • Hounsell, E.F.1    Davies, M.J.2    Smith, K.D.3
  • 17
    • 36148974441 scopus 로고    scopus 로고
    • Enrichment and analysis of glycoproteins in the proteome
    • G.B. Smejkal, A. Lazarev, CRC Press Boca Raton, FL
    • N.L. Wilson, N.G. Karlsson, and N.H. Packer Enrichment and analysis of glycoproteins in the proteome G.B. Smejkal, A. Lazarev, Separation methods in proteomics 2006 CRC Press Boca Raton, FL 350 355
    • (2006) Separation Methods in Proteomics , pp. 350-355
    • Wilson, N.L.1    Karlsson, N.G.2    Packer, N.H.3
  • 18
    • 84871693371 scopus 로고
    • The spectrophotometric determination of tyrosine and tryptophan in proteins
    • W. Goodwin, and R.A. Morton The spectrophotometric determination of tyrosine and tryptophan in proteins Biochem J 40 1946 628 632
    • (1946) Biochem J , vol.40 , pp. 628-632
    • Goodwin, W.1    Morton, R.A.2
  • 19
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • L. Ellman Tissue sulfhydryl groups Arch Biochem Biophys 82 1959 70 77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, L.1
  • 20
    • 0012382504 scopus 로고    scopus 로고
    • Protein determination by UV absorption
    • J.M. Walker, Humana Press Totowa, NJ
    • A. Aitken, and M. Learmonth Protein determination by UV absorption J.M. Walker, The protein protocols handbook 1997 Humana Press Totowa, NJ 3 6
    • (1997) The Protein Protocols Handbook , pp. 3-6
    • Aitken, A.1    Learmonth, M.2
  • 21
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • B.F. Erlanger, N. Kokowsky, and N. Cohen The preparation and properties of two new chromogenic substrates of trypsin Arch Biochem Biophys 95 1961 271 278
    • (1961) Arch Biochem Biophys , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, N.3
  • 23
    • 0032716420 scopus 로고    scopus 로고
    • Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive
    • DOI 10.1016/S0032-9592(99)00053-9, PII S0032959299000539
    • U.C. Banerjee, R.K. Sani, W. Azmi, and R. Sani Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive Process Biochem 35 1999 213 219 (Pubitemid 29513210)
    • (1999) Process Biochemistry , vol.35 , Issue.1-2 , pp. 213-219
    • Banerjee, U.C.1    Sani, R.K.2    Azmi, W.3    Soni, R.4
  • 24
    • 0001442231 scopus 로고
    • Milk-clotting enzyme from Mucor pusillus var. Lindt
    • G. Pearlman, L. Lorand, Academic Press New York
    • K. Arima, J. Yu, and S. Iwasaki Milk-clotting enzyme from Mucor pusillus var. Lindt G. Pearlman, L. Lorand, Methods in enzymology 1970 Academic Press New York 446 459
    • (1970) Methods in Enzymology , pp. 446-459
    • Arima, K.1    Yu, J.2    Iwasaki, S.3
  • 25
    • 0000154726 scopus 로고
    • Immunodiffusion and immunoelectrophoresis
    • D.M. Weir, L.A. Herzerberg, C. Blackwell, L.A. Herzerberg, Blackwell Oxford
    • O. Ouchterlony, and L.A. Nilsson Immunodiffusion and immunoelectrophoresis D.M. Weir, L.A. Herzerberg, C. Blackwell, L.A. Herzerberg, Handbook of experimental immunology 1986 Blackwell Oxford 32.1 32.50
    • (1986) Handbook of Experimental Immunology , pp. 321-3250
    • Ouchterlony, O.1    Nilsson, L.A.2
  • 26
    • 33746189464 scopus 로고    scopus 로고
    • Highly stable glycosylated serine protease from the medicinal plant Euphorbia milii
    • DOI 10.1016/j.phytochem.2006.06.002, PII S0031942206003189
    • S.C. Yadav, M. Pande, and M.V. Jagannadham Highly stable glycosylated serine protease from the medicinal plant Euphorbia milli Phytochemistry 67 2006 1414 1426 (Pubitemid 44092926)
    • (2006) Phytochemistry , vol.67 , Issue.14 , pp. 1414-1426
    • Yadav, S.C.1    Pande, M.2    Jagannadham, M.V.3
  • 27
    • 48049104106 scopus 로고    scopus 로고
    • Indicain, a dimeric serine protease from Morus indica cv K2
    • V.K. Singh, A.K. Patel, A.J. Moir, and M.V. Jagannadham Indicain, a dimeric serine protease from Morus indica cv K2 Phytochemistry 69 2008 2110 2119
    • (2008) Phytochemistry , vol.69 , pp. 2110-2119
    • Singh, V.K.1    Patel, A.K.2    Moir, A.J.3    Jagannadham, M.V.4
  • 31
    • 0028112093 scopus 로고
    • Purification and characterization of an endoprotease from melon fruit
    • K. Noda, M. Koyanagi, and C. Kamiya Purification and characterization of an endoprotease from melon fruit J Food Sci 59 1994 585 587 (Pubitemid 2116163)
    • (1994) Journal of Food Science , vol.59 , Issue.3 , pp. 585-587
    • Noda, K.1    Koyanagi, M.2    Kamiya, C.3
  • 32
    • 23644445987 scopus 로고    scopus 로고
    • Glucosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics
    • DOI 10.1110/ps.051405005
    • M.M.A. Van Teeffelen, K. Broersen, and H.J. De Jongh Glucosylation of b-lactoglobulin lowers the capacity change of unfolding, a unique way to affect protein thermodynamics Protein Sci 14 2005 2187 2194 (Pubitemid 41132383)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2187-2194
    • Van Teeffelen, A.M.M.1    Broersen, K.2    De Jongh, H.H.J.3
  • 33
    • 70449678591 scopus 로고    scopus 로고
    • Crinumin, a chymotrypsin-like but glycosylated serine protease from Crinum asiaticum: Purification and physicochemical characterization
    • K.A. Singh, R. Kumar, G.R.K. Rao, and M.V. Jagannadham Crinumin, a chymotrypsin-like but glycosylated serine protease from Crinum asiaticum: purification and physicochemical characterization Food Chem 119 2010 1352 1358
    • (2010) Food Chem , vol.119 , pp. 1352-1358
    • Singh, K.A.1    Kumar, R.2    Rao, G.R.K.3    Jagannadham, M.V.4
  • 34
    • 0028990247 scopus 로고
    • Cleavage specificity of cucumisin, a plant serine protease
    • T. Uchikoba, H. Yonezawa, and M. Kaneda Cleavage specificity of cucumisin, a plant serine protease J Biochem 117 1995 1126 1130
    • (1995) J Biochem , vol.117 , pp. 1126-1130
    • Uchikoba, T.1    Yonezawa, H.2    Kaneda, M.3
  • 35
    • 0034622529 scopus 로고    scopus 로고
    • Isolation and characterization of a serine protease from the sprouts of Pleioblastus hindsii Nakai
    • DOI 10.1016/S0031-9422(00)00075-3, PII S0031942200000753
    • K Arima, T. Uchikoba, H. Yonezawa, M. Shimada, and M. Kaneda Isolation and characterization of a serine protease from the sprouts of Pleioblastus hindsii Nakai Phytochemistry 54 2000 559 565 (Pubitemid 30625829)
    • (2000) Phytochemistry , vol.54 , Issue.6 , pp. 559-565
    • Arima, K.1    Uchikoba, T.2    Yonezawa, H.3    Shimada, M.4    Kaneda, M.5
  • 36
    • 62549122479 scopus 로고    scopus 로고
    • Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen
    • I.A.M. Ahmed, I. Morishima, E.E. Babiker, and N. Mori Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen Phytochemistry 70 2009 483 491
    • (2009) Phytochemistry , vol.70 , pp. 483-491
    • Ahmed, I.A.M.1    Morishima, I.2    Babiker, E.E.3    Mori, N.4
  • 37
    • 0023134530 scopus 로고
    • Production and activation of SDS resistant alkaline serine exoprotease of Vibrio alginolyticus
    • S.M. Deane, F.T. Robb, and D.R. Woods Production and activation of SDS resistant alkaline serine exoprotease of Vibrio alginolyticus J Gen Microbiol 133 1987 272 294
    • (1987) J Gen Microbiol , vol.133 , pp. 272-294
    • Deane, S.M.1    Robb, F.T.2    Woods, D.R.3
  • 38
    • 0034769033 scopus 로고    scopus 로고
    • Characterization and wash performance analysis of an SDS-stable alkaline protease from a Bacillus sp
    • DOI 10.1023/A:1011918806201
    • R. Oberoi, Q.K. Beg, S. Puri, R.K. Saxena, and R. Gupta Characterization and wash performance analysis of an SDS-stable alkaline protease from a Bacillus sp World J Microbiol Biotechnol 17 2001 493 497 (Pubitemid 32990356)
    • (2001) World Journal of Microbiology and Biotechnology , vol.17 , Issue.5 , pp. 493-497
    • Oberoi, R.1    Beg, Q.K.2    Puri, S.3    Saxena, R.K.4    Gupta, R.5
  • 39
    • 3342881957 scopus 로고    scopus 로고
    • Production, purification and characterization of a novel thermo stable serine protease from soil isolate Streptomyces tendae
    • C.N. Seong, J.S. Jo, S.K. Choi, S.W. Kim, S.J. Kim, and O.H. Lee Production, purification and characterization of a novel thermo stable serine protease from soil isolate Streptomyces tendae Biotechnol Lett 26 2004 907 909
    • (2004) Biotechnol Lett , vol.26 , pp. 907-909
    • Seong, C.N.1    Jo, J.S.2    Choi, S.K.3    Kim, S.W.4    Kim, S.J.5    Lee, O.H.6
  • 40
    • 0038301954 scopus 로고    scopus 로고
    • Purification and characterization of a protease from solid state cultures of Aspergillus parasiticus
    • DOI 10.1016/S0032-9592(03)00048-7
    • R. Tunga, B. Shrivastava, and R. Banerjee Purification and characterization of a protease from solid-state cultures of Aspergillus parasiticus Process Biochem 38 2003 1553 1558 (Pubitemid 36821287)
    • (2003) Process Biochemistry , vol.38 , Issue.11 , pp. 1553-1558
    • Tunga, R.1    Shrivastava, B.2    Banerjee, R.3
  • 43
    • 33750495382 scopus 로고    scopus 로고
    • Purification and characterization of a 34-kDa, heat stable glycoprotein from Synadenium grantii latex: action on human fibrinogen and fibrin clot
    • DOI 10.1016/j.biochi.2006.06.007, PII S0300908406001088
    • R. Rajesh, A. Nataraju, C.D.R. Gowda, B.M. Frey, F.J. Frey, and B.S. Vishwanath Purification and characterization of a 34-kDa, heat stable glycoprotein from Synadenium grantii latex: action on human fibrinogen and fibrin clot Biochimie 88 2006 1313 1322 (Pubitemid 44667219)
    • (2006) Biochimie , vol.88 , Issue.10 , pp. 1313-1322
    • Rajesh, R.1    Nataraju, A.2    Gowda, C.D.R.3    Frey, B.M.4    Frey, F.J.5    Vishwanath, B.S.6
  • 44
    • 0028587825 scopus 로고
    • Cucumisin, a serine protease from melon fruit, shares structural homology with subtilisin and is generated from a large precursor
    • H. Yagamata, T. Masuzawa, Y. Nagaoka, T. Ohnishi, and T. Iwasaki Cucumisin, a serine protease from melon fruit, shares structural homology with subtilisin and is generated from a large precursor J Biol Chem 260 1994 32725 32731
    • (1994) J Biol Chem , vol.260 , pp. 32725-32731
    • Yagamata, H.1    Masuzawa, T.2    Nagaoka, Y.3    Ohnishi, T.4    Iwasaki, T.5
  • 45
    • 0029900079 scopus 로고    scopus 로고
    • Primary structure and expression of a pathogen induced protease (PR-P69) in tomato plants
    • P Tornero, V. Conezaro, and P. Vera Primary structure and expression of a pathogen induced protease (PR-P69) in tomato plants Proc Natl Acad Sci USA 93 1996 6332 6337
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6332-6337
    • Tornero, P.1    Conezaro, V.2    Vera, P.3
  • 46
    • 0030970430 scopus 로고    scopus 로고
    • Identification of a new pathogen-induced member of the subtilisin-like processing protease family from plants
    • DOI 10.1074/jbc.272.22.14412
    • P. Tornero, ConezaroV, and P. Vera Identification of a new pathogen induced member of the subtilisin-like processing protease family from plants J Biol Chem 272 1997 14412 14419 (Pubitemid 27232859)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14412-14419
    • Tornero, P.1    Conejero, V.2    Vera, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.