메뉴 건너뛰기




Volumn 118, Issue 6, 2014, Pages 622-627

Identification, purification and characterization of a novel collagenolytic serine protease from fig (Ficus carica var. Brown Turkey) latex

Author keywords

Collagenolytic activity; Enzyme purification; Fig latex; Gelatinolytic activity; Serine protease

Indexed keywords

AMINO ACIDS; GEL PERMEATION CHROMATOGRAPHY; PURIFICATION; VALUE ENGINEERING;

EID: 84922819521     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2014.05.020     Document Type: Article
Times cited : (43)

References (39)
  • 1
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr. Opin. Cell Biol. 1995, 7:728-735.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 2
    • 77953897406 scopus 로고    scopus 로고
    • Mechanism of the calcium-induced trans-cis isomerization of a non-prolyl peptide bond in Clostridium histolyticum collagenase
    • Spiriti J., Van der Vaart A. Mechanism of the calcium-induced trans-cis isomerization of a non-prolyl peptide bond in Clostridium histolyticum collagenase. Biochemistry 2010, 49:5314-5320.
    • (2010) Biochemistry , vol.49 , pp. 5314-5320
    • Spiriti, J.1    Van der Vaart, A.2
  • 4
    • 0019331559 scopus 로고
    • Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates
    • Grant G.A., Eisen A.Z. Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with noncollagenous substrates. Biochemistry 1980, 19:6089-6095.
    • (1980) Biochemistry , vol.19 , pp. 6089-6095
    • Grant, G.A.1    Eisen, A.Z.2
  • 5
    • 0026460104 scopus 로고
    • Purification, biochemical characterization and N-terminal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda)
    • Van Wormhoudt A., Le Chevalier P., Sellos D. Purification, biochemical characterization and N-terminal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda). Comp. Biochem. Physiol. B 1992, 103:675-680.
    • (1992) Comp. Biochem. Physiol. B , vol.103 , pp. 675-680
    • Van Wormhoudt, A.1    Le Chevalier, P.2    Sellos, D.3
  • 6
    • 0000051107 scopus 로고
    • Tenderization of beef with bacterial collagenase
    • Foegeding E.A., Larick D.K. Tenderization of beef with bacterial collagenase. Meat Sci. 1986, 18:201-214.
    • (1986) Meat Sci. , vol.18 , pp. 201-214
    • Foegeding, E.A.1    Larick, D.K.2
  • 8
    • 39549098706 scopus 로고    scopus 로고
    • Establishment of fibroblast cultures
    • John Wiley & Sons, Inc., New York, J.S. Bonifacino, M. Dasso, J.B. Harford, J.,. Lippincott-Schwartz, K.M. Yamada (Eds.)
    • Takashima A. Establishment of fibroblast cultures. Current protocols in cell biology 2001, 2.1.1-2.1.12. John Wiley & Sons, Inc., New York. J.S. Bonifacino, M. Dasso, J.B. Harford, J.,. Lippincott-Schwartz, K.M. Yamada (Eds.).
    • (2001) Current protocols in cell biology
    • Takashima, A.1
  • 9
    • 0029257201 scopus 로고
    • Use of standardized protease enzymes for antibody screening of blood donor samples with the microplate system AutoAnalyzer
    • Mazda T., Makino K., Yabe R., Nakata K., Fujisawa K., Ohshima H. Use of standardized protease enzymes for antibody screening of blood donor samples with the microplate system AutoAnalyzer. Transfus. Med. 1995, 5:43-50.
    • (1995) Transfus. Med. , vol.5 , pp. 43-50
    • Mazda, T.1    Makino, K.2    Yabe, R.3    Nakata, K.4    Fujisawa, K.5    Ohshima, H.6
  • 11
    • 84888003578 scopus 로고    scopus 로고
    • Clinical and economic assessment of diabetic foot ulcer debridement with collagenase: results of a randomized controlled study
    • Tallis A., Motley T.A., Wunderlich R.P., Dickerson J.E., Waycaster C., Slade H.B. Clinical and economic assessment of diabetic foot ulcer debridement with collagenase: results of a randomized controlled study. Clin. Ther. 2013, 35:1805-1820.
    • (2013) Clin. Ther. , vol.35 , pp. 1805-1820
    • Tallis, A.1    Motley, T.A.2    Wunderlich, R.P.3    Dickerson, J.E.4    Waycaster, C.5    Slade, H.B.6
  • 14
    • 33846226474 scopus 로고    scopus 로고
    • Factors influencing the collagenase digestion phase of human islet isolation
    • Kin T., Johnson P.R., Shapiro A.M., Lakey J.R. Factors influencing the collagenase digestion phase of human islet isolation. Transplantation 2007, 83:7-12.
    • (2007) Transplantation , vol.83 , pp. 7-12
    • Kin, T.1    Johnson, P.R.2    Shapiro, A.M.3    Lakey, J.R.4
  • 15
    • 78751643426 scopus 로고    scopus 로고
    • Tissue dissociation enzymes for isolating human islets for transplantation: factors to consider in setting enzyme acceptance criteria
    • McCarthy R.C., Breite A.G., Green M.L., Dwulet F.E. Tissue dissociation enzymes for isolating human islets for transplantation: factors to consider in setting enzyme acceptance criteria. Transplantation 2011, 91:137-145.
    • (2011) Transplantation , vol.91 , pp. 137-145
    • McCarthy, R.C.1    Breite, A.G.2    Green, M.L.3    Dwulet, F.E.4
  • 16
    • 84887083089 scopus 로고    scopus 로고
    • Baseline characteristics from an ongoing phase 3 study of collagenase Clostridium histolyticum in patients with Peyronie's disease
    • Gelbard M., Hellstrom W.J., McMahon C.G., Levine L.A., Smith T., Tursi J., Kaufman G., Goldstein I. Baseline characteristics from an ongoing phase 3 study of collagenase Clostridium histolyticum in patients with Peyronie's disease. J.Sex. Med. 2013, 10:2822-2831.
    • (2013) J.Sex. Med. , vol.10 , pp. 2822-2831
    • Gelbard, M.1    Hellstrom, W.J.2    McMahon, C.G.3    Levine, L.A.4    Smith, T.5    Tursi, J.6    Kaufman, G.7    Goldstein, I.8
  • 18
    • 32544441439 scopus 로고    scopus 로고
    • Bioactive compounds from marine processing byproducts - a review
    • Kim S.K., Mendis E. Bioactive compounds from marine processing byproducts - a review. Food Res. Int. 2006, 39:383-393.
    • (2006) Food Res. Int. , vol.39 , pp. 383-393
    • Kim, S.K.1    Mendis, E.2
  • 19
    • 35448933148 scopus 로고    scopus 로고
    • Plant collagenase: unique collagenolytic activity of cysteine proteases from ginger
    • Kim M., Hamilton S.E., Guddat L.W., Overall C.M. Plant collagenase: unique collagenolytic activity of cysteine proteases from ginger. Biochim. Biophys. Acta 2007, 1770:1627-1635.
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 1627-1635
    • Kim, M.1    Hamilton, S.E.2    Guddat, L.W.3    Overall, C.M.4
  • 20
    • 58949090489 scopus 로고    scopus 로고
    • Purification, characterization, and solvent-induced thermal stabilization of ficin from Ficus carica
    • Devaraj K.B., Kumar P.R., Prakash V. Purification, characterization, and solvent-induced thermal stabilization of ficin from Ficus carica. J.Agric. Food Chem. 2008, 56:11417-11423.
    • (2008) J.Agric. Food Chem. , vol.56 , pp. 11417-11423
    • Devaraj, K.B.1    Kumar, P.R.2    Prakash, V.3
  • 21
    • 0034910124 scopus 로고    scopus 로고
    • Suppressors of cancer cell proliferation from fig (Ficus carica) resin: isolation and structure elucidation
    • Rubnov S., Kashman Y., Rabinowitz R., Schlesinger M., Mechoulam R. Suppressors of cancer cell proliferation from fig (Ficus carica) resin: isolation and structure elucidation. J.Nat. Prod. 2001, 64:993-996.
    • (2001) J.Nat. Prod. , vol.64 , pp. 993-996
    • Rubnov, S.1    Kashman, Y.2    Rabinowitz, R.3    Schlesinger, M.4    Mechoulam, R.5
  • 23
    • 78651158997 scopus 로고
    • Ficus enzymes: I. separation of the proteolytic enzymes of Ficus carica and Ficus glabrata latices
    • Sgarbieri V.C., Gupte S.M., Kramer D.E., Whitaker J.R. Ficus enzymes: I. separation of the proteolytic enzymes of Ficus carica and Ficus glabrata latices. J.Biol. Chem. 1964, 239:2170-2177.
    • (1964) J.Biol. Chem. , vol.239 , pp. 2170-2177
    • Sgarbieri, V.C.1    Gupte, S.M.2    Kramer, D.E.3    Whitaker, J.R.4
  • 25
    • 0017170235 scopus 로고
    • Preparation of fully active ficin from Ficus glabrata by covalent chromatography and characterization of its active centre by using 2,2'-depyridyl disulphide as a reactivity probe
    • Malthouse J.P., Brocklehurst K. Preparation of fully active ficin from Ficus glabrata by covalent chromatography and characterization of its active centre by using 2,2'-depyridyl disulphide as a reactivity probe. Biochem. J. 1976, 159:221-234.
    • (1976) Biochem. J. , vol.159 , pp. 221-234
    • Malthouse, J.P.1    Brocklehurst, K.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0002184935 scopus 로고    scopus 로고
    • Isoelectric focusing and two-dimensional gel electrophoresis
    • Wiley-Liss, New York, D.M. Bollag, M.D.,. Rozycki, S.J. Edelstein (Eds.)
    • Bollag D.M. Isoelectric focusing and two-dimensional gel electrophoresis. Protein methods 1996, 173-194. Wiley-Liss, New York. 2nd ed. D.M. Bollag, M.D.,. Rozycki, S.J. Edelstein (Eds.).
    • (1996) Protein methods , pp. 173-194
    • Bollag, D.M.1
  • 29
    • 84875962519 scopus 로고    scopus 로고
    • Astraightforward ninhydrin-based method for collagenase activity and inhibitor screening of collagenase using spectrophotometry
    • Zhang Y., Fun Y., Zhou S., Kang L., Li C. Astraightforward ninhydrin-based method for collagenase activity and inhibitor screening of collagenase using spectrophotometry. Anal. Biochem. 2013, 437:46-48.
    • (2013) Anal. Biochem. , vol.437 , pp. 46-48
    • Zhang, Y.1    Fun, Y.2    Zhou, S.3    Kang, L.4    Li, C.5
  • 30
    • 84982334950 scopus 로고
    • The ficin content of the latex from different varieties of Ficus carica and a comparison of several micro-methods of protein determination
    • Whitaker J.R. The ficin content of the latex from different varieties of Ficus carica and a comparison of several micro-methods of protein determination. J.Food Sci. 1958, 23:364-370.
    • (1958) J.Food Sci. , vol.23 , pp. 364-370
    • Whitaker, J.R.1
  • 31
    • 0343167441 scopus 로고    scopus 로고
    • Identification of natural rubber and characterization of rubber biosynthetic activity in fig tree
    • Kang H., Kang M.Y., Han K.H. Identification of natural rubber and characterization of rubber biosynthetic activity in fig tree. Plant Physiol. 2000, 123:1133-1142.
    • (2000) Plant Physiol. , vol.123 , pp. 1133-1142
    • Kang, H.1    Kang, M.Y.2    Han, K.H.3
  • 33
    • 0000412597 scopus 로고
    • Isolation and characterization of proteinase and collagenase from Cl. histolyticum
    • Mandl I., MacLennan J.D., Howes E.L., DeBellis R.H., Sohler A. Isolation and characterization of proteinase and collagenase from Cl. histolyticum. J.Clin. Invest. 1953, 32:1323-1329.
    • (1953) J.Clin. Invest. , vol.32 , pp. 1323-1329
    • Mandl, I.1    MacLennan, J.D.2    Howes, E.L.3    DeBellis, R.H.4    Sohler, A.5
  • 35
    • 1842870680 scopus 로고    scopus 로고
    • Purification and characterization of a collagenase from the mackerel, Scomber japonicus
    • Park P.J., Lee S.H., Byun H.G., Kim S.H., Kim S.K. Purification and characterization of a collagenase from the mackerel, Scomber japonicus. J.Biochem. Mol. Biol. 2002, 35:576-582.
    • (2002) J.Biochem. Mol. Biol. , vol.35 , pp. 576-582
    • Park, P.J.1    Lee, S.H.2    Byun, H.G.3    Kim, S.H.4    Kim, S.K.5
  • 36
    • 77954548440 scopus 로고    scopus 로고
    • Decolorization of crude latex by activated charcoal, purification and physico-chemical characterization of religiosin, a milk-clotting serine protease from the latex of Ficus religiosa
    • Kumari M., Sharma A., Jagannadham M.V. Decolorization of crude latex by activated charcoal, purification and physico-chemical characterization of religiosin, a milk-clotting serine protease from the latex of Ficus religiosa. J.Agric. Food Chem. 2010, 58:8027-8034.
    • (2010) J.Agric. Food Chem. , vol.58 , pp. 8027-8034
    • Kumari, M.1    Sharma, A.2    Jagannadham, M.V.3
  • 37
    • 72449194286 scopus 로고    scopus 로고
    • Benghalensin, a highly stable serine protease from the latex of medicinal plant Ficus benghalensis
    • Sharma A., Kumari M., Jagannadham M.V. Benghalensin, a highly stable serine protease from the latex of medicinal plant Ficus benghalensis. J.Agric. Food Chem. 2009, 57:11120-11126.
    • (2009) J.Agric. Food Chem. , vol.57 , pp. 11120-11126
    • Sharma, A.1    Kumari, M.2    Jagannadham, M.V.3
  • 38
    • 51049083362 scopus 로고    scopus 로고
    • Ficus spp. (fig): ethnobotany and potential as anticancer and anti-inflammatory agents
    • Lansky E.P., Paavilainen H.M., Pawlus A.D., Newman R.A. Ficus spp. (fig): ethnobotany and potential as anticancer and anti-inflammatory agents. J.Ethnopharmacol. 2008, 119:195-213.
    • (2008) J.Ethnopharmacol. , vol.119 , pp. 195-213
    • Lansky, E.P.1    Paavilainen, H.M.2    Pawlus, A.D.3    Newman, R.A.4
  • 39
    • 84864999405 scopus 로고    scopus 로고
    • Proteolytic enzymes of some laticiferous plants belonging to Khandesh region of Maharashtra, India
    • Badgujar S.B.M., Mahajan R.T. Proteolytic enzymes of some laticiferous plants belonging to Khandesh region of Maharashtra, India. J.Pharm. Res. 2009, 2:1434-1437.
    • (2009) J.Pharm. Res. , vol.2 , pp. 1434-1437
    • Badgujar, S.B.M.1    Mahajan, R.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.