메뉴 건너뛰기




Volumn 13, Issue 1, 2014, Pages

Highly purified mussel adhesive protein to secure biosafety for in vivo applications

Author keywords

Biosafety; Endotoxin; Gram negative Escherichia coli; High resolution purification; In vivo standard; Lipopolysaccharide; Mussel adhesive protein

Indexed keywords

ENDOTOXIN; INTERLEUKIN 6; MUSSEL ADHESIVE PROTEIN; RECOMBINANT FP 151 PROTEIN; RECOMBINANT PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84899645547     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-13-52     Document Type: Article
Times cited : (43)

References (30)
  • 1
    • 0021099316 scopus 로고
    • Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L
    • Waite JH. Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L. J Biol Chem 1983, 258:2911-2915.
    • (1983) J Biol Chem , vol.258 , pp. 2911-2915
    • Waite, J.H.1
  • 2
  • 3
    • 36749099994 scopus 로고    scopus 로고
    • Understanding marine mussel adhesion
    • 10.1007/s10126-007-9053-x, 2100433, 17990038
    • Silverman HG, Roberto FF. Understanding marine mussel adhesion. Mar Biotechnol (NY) 2007, 9:661-681. 10.1007/s10126-007-9053-x, 2100433, 17990038.
    • (2007) Mar Biotechnol (NY) , vol.9 , pp. 661-681
    • Silverman, H.G.1    Roberto, F.F.2
  • 4
    • 0022737072 scopus 로고
    • Adhesive protein from mussels: possibilities for dentistry, medicine, and industry
    • Dove J, Sheridan P. Adhesive protein from mussels: possibilities for dentistry, medicine, and industry. J Am Dent Assoc 1986, 112:879.
    • (1986) J Am Dent Assoc , vol.112 , pp. 879
    • Dove, J.1    Sheridan, P.2
  • 5
    • 0038067927 scopus 로고    scopus 로고
    • Adhesion a la moule
    • 10.1093/icb/42.6.1172, 21680402
    • Waite JH. Adhesion a la moule. Integr Comp Biol 2002, 42:1172-1180. 10.1093/icb/42.6.1172, 21680402.
    • (2002) Integr Comp Biol , vol.42 , pp. 1172-1180
    • Waite, J.H.1
  • 6
    • 77957311585 scopus 로고    scopus 로고
    • Cell behavior on extracellular matrix mimic materials based on mussel adhesive protein fused with functional peptides
    • 10.1016/j.biomaterials.2010.08.027, 20832110
    • Choi B-H, Choi YS, Kang DG, Kim BJ, Song YH, Cha HJ. Cell behavior on extracellular matrix mimic materials based on mussel adhesive protein fused with functional peptides. Biomaterials 2010, 31:8980-8988. 10.1016/j.biomaterials.2010.08.027, 20832110.
    • (2010) Biomaterials , vol.31 , pp. 8980-8988
    • Choi, B.-H.1    Choi, Y.S.2    Kang, D.G.3    Kim, B.J.4    Song, Y.H.5    Cha, H.J.6
  • 7
    • 84862908766 scopus 로고    scopus 로고
    • Reinforced multifunctionalized nanofibrous scaffolds using mussel adhesive proteins
    • Kim BJ, Choi YS, Cha HJ. Reinforced multifunctionalized nanofibrous scaffolds using mussel adhesive proteins. Angew Chem Int Ed 2012, 51:675-678.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 675-678
    • Kim, B.J.1    Choi, Y.S.2    Cha, H.J.3
  • 8
    • 0025428789 scopus 로고
    • Structural and functional repetition in a marine mussel adhesive protein
    • 10.1021/bp00003a001, 1367451
    • Filpula DR, Lee SM, Link RP, Strausberg SL, Strausberg RL. Structural and functional repetition in a marine mussel adhesive protein. Biotechnol Prog 1990, 6:171-177. 10.1021/bp00003a001, 1367451.
    • (1990) Biotechnol Prog , vol.6 , pp. 171-177
    • Filpula, D.R.1    Lee, S.M.2    Link, R.P.3    Strausberg, S.L.4    Strausberg, R.L.5
  • 9
    • 0027312161 scopus 로고
    • Cloning, expression, and characterization of a synthetic analog to the bioadhesive precursor protein of the sea mussel Mytilus edulis
    • Salerno AJ, Goldberg I. Cloning, expression, and characterization of a synthetic analog to the bioadhesive precursor protein of the sea mussel Mytilus edulis. Appl Microbiol Biotechnol 1993, 39:221-226.
    • (1993) Appl Microbiol Biotechnol , vol.39 , pp. 221-226
    • Salerno, A.J.1    Goldberg, I.2
  • 10
    • 2942532196 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli
    • 10.1128/AEM.70.6.3352-3359.2004, 427802, 15184131
    • Hwang DS, Yoo HJ, Jun JH, Moon WK, Cha HJ. Expression of functional recombinant mussel adhesive protein Mgfp-5 in Escherichia coli. Appl Environ Microbiol 2004, 70:3352-3359. 10.1128/AEM.70.6.3352-3359.2004, 427802, 15184131.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3352-3359
    • Hwang, D.S.1    Yoo, H.J.2    Jun, J.H.3    Moon, W.K.4    Cha, H.J.5
  • 11
    • 20144366711 scopus 로고    scopus 로고
    • Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli
    • Hwang DS, Gim Y, Cha HJ. Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli. Biotechnol Prog 2005, 21:965-970.
    • (2005) Biotechnol Prog , vol.21 , pp. 965-970
    • Hwang, D.S.1    Gim, Y.2    Cha, H.J.3
  • 12
    • 44949138865 scopus 로고    scopus 로고
    • Development of bioadhesives from marine mussels
    • 10.1002/biot.200700258, 18293310
    • Cha HJ, Hwang DS, Lim S. Development of bioadhesives from marine mussels. Biotechnol J 2008, 3:631-638. 10.1002/biot.200700258, 18293310.
    • (2008) Biotechnol J , vol.3 , pp. 631-638
    • Cha, H.J.1    Hwang, D.S.2    Lim, S.3
  • 13
    • 34249307818 scopus 로고    scopus 로고
    • Practical recombinant hybrid mussel bioadhesive fp-151
    • 10.1016/j.biomaterials.2007.04.039, 17507090
    • Hwang DS, Gim Y, Yoo HJ, Cha HJ. Practical recombinant hybrid mussel bioadhesive fp-151. Biomaterials 2007, 28:3560-3568. 10.1016/j.biomaterials.2007.04.039, 17507090.
    • (2007) Biomaterials , vol.28 , pp. 3560-3568
    • Hwang, D.S.1    Gim, Y.2    Yoo, H.J.3    Cha, H.J.4
  • 14
    • 77956626926 scopus 로고    scopus 로고
    • Endotoxins: lipopolysaccharides of gram-negative bacteria
    • 10.1007/978-90-481-9078-2_1, 20593260
    • Wang X, Quinn PJ. Endotoxins: lipopolysaccharides of gram-negative bacteria. Subcell Biochem 2010, 53:3-25. 10.1007/978-90-481-9078-2_1, 20593260.
    • (2010) Subcell Biochem , vol.53 , pp. 3-25
    • Wang, X.1    Quinn, P.J.2
  • 16
    • 0037414787 scopus 로고    scopus 로고
    • Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor a release by murine macrophages
    • Gao BC, Tsan MF. Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor a release by murine macrophages. J Biol Chem 2003, 278:174-179.
    • (2003) J Biol Chem , vol.278 , pp. 174-179
    • Gao, B.C.1    Tsan, M.F.2
  • 18
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • 10.1016/S0168-1656(99)00185-6, 10656326
    • Petsch D, Anspach FB. Endotoxin removal from protein solutions. J Biotechnol 2000, 76:97-119. 10.1016/S0168-1656(99)00185-6, 10656326.
    • (2000) J Biotechnol , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2
  • 19
    • 0030882663 scopus 로고    scopus 로고
    • Removal of endotoxin from recombinant protein preparations
    • 10.1016/S0009-9120(97)00049-0, 9316739
    • Liu S, Tobias R, McClure S, Styba G, Shi Q, Jackowski G. Removal of endotoxin from recombinant protein preparations. Clin Biochem 1997, 30:455-463. 10.1016/S0009-9120(97)00049-0, 9316739.
    • (1997) Clin Biochem , vol.30 , pp. 455-463
    • Liu, S.1    Tobias, R.2    McClure, S.3    Styba, G.4    Shi, Q.5    Jackowski, G.6
  • 20
    • 0035370666 scopus 로고    scopus 로고
    • Removal of tightly bound endotoxin from biological products
    • 10.1016/S0168-1656(01)00256-5, 11377766
    • Wilson MJ, Haggart CL, Gallagher SP, Walsh D. Removal of tightly bound endotoxin from biological products. J Biotechnol 2001, 88:67-75. 10.1016/S0168-1656(01)00256-5, 11377766.
    • (2001) J Biotechnol , vol.88 , pp. 67-75
    • Wilson, M.J.1    Haggart, C.L.2    Gallagher, S.P.3    Walsh, D.4
  • 21
    • 33645409827 scopus 로고    scopus 로고
    • Single step protocol to purify recombinant proteins with low endotoxin contents
    • 10.1016/j.pep.2005.09.027, 16290005
    • Reichelt P, Schwarz C, Donzeau M. Single step protocol to purify recombinant proteins with low endotoxin contents. Protein Expr Purif 2006, 46:483-488. 10.1016/j.pep.2005.09.027, 16290005.
    • (2006) Protein Expr Purif , vol.46 , pp. 483-488
    • Reichelt, P.1    Schwarz, C.2    Donzeau, M.3
  • 22
    • 78651253185 scopus 로고    scopus 로고
    • Factors affecting endotoxin removal from aqueous solutions by ultrafiltration process
    • El-Moghazy ANA. Factors affecting endotoxin removal from aqueous solutions by ultrafiltration process. J Sci Ind Res (India) 2011, 70:55-59.
    • (2011) J Sci Ind Res (India) , vol.70 , pp. 55-59
    • El-Moghazy, A.N.A.1
  • 23
    • 84859034602 scopus 로고    scopus 로고
    • Removing endotoxin from plasmid samples by Triton X-114 isothermal extraction
    • 10.1016/j.ab.2012.02.015, 22370278
    • Ma R, Zhao J, Du HC, Tian S, Li L-W. Removing endotoxin from plasmid samples by Triton X-114 isothermal extraction. Anal Biochem 2012, 424:124-126. 10.1016/j.ab.2012.02.015, 22370278.
    • (2012) Anal Biochem , vol.424 , pp. 124-126
    • Ma, R.1    Zhao, J.2    Du, H.C.3    Tian, S.4    Li, L.-W.5
  • 24
    • 0021211109 scopus 로고
    • Advantages and limitations of density gradient ultracentrifugation in the fractionation of human serum lipoproteins: role of salts and sucrose
    • Edelstein C, Pfaffinger D, Scanu AM. Advantages and limitations of density gradient ultracentrifugation in the fractionation of human serum lipoproteins: role of salts and sucrose. J Lipid Res 1984, 25:630-637.
    • (1984) J Lipid Res , vol.25 , pp. 630-637
    • Edelstein, C.1    Pfaffinger, D.2    Scanu, A.M.3
  • 25
    • 0014430361 scopus 로고
    • Physical, chemical, and immunological properties of lipopolysaccharide released from Escherichia coli by ethylenediaminetetraacetate
    • Leive L, Shovlin VK, Mergenhagen SE. Physical, chemical, and immunological properties of lipopolysaccharide released from Escherichia coli by ethylenediaminetetraacetate. J Biol Chem 1968, 243:6384-6391.
    • (1968) J Biol Chem , vol.243 , pp. 6384-6391
    • Leive, L.1    Shovlin, V.K.2    Mergenhagen, S.E.3
  • 26
    • 0016138377 scopus 로고
    • The barrier function of the gram-negative envelope
    • 10.1111/j.1749-6632.1974.tb43261.x, 4212391
    • Leive L. The barrier function of the gram-negative envelope. Ann N Y Acad Sci 1974, 235:109-129. 10.1111/j.1749-6632.1974.tb43261.x, 4212391.
    • (1974) Ann N Y Acad Sci , vol.235 , pp. 109-129
    • Leive, L.1
  • 28
    • 79959264028 scopus 로고    scopus 로고
    • Hofmeister series salts enhance purification of plasmid DNA by non-ionic detergents
    • 10.1002/bit.23116, 3117116, 21351074
    • Lezin G, Kuehn MR, Brunelli L. Hofmeister series salts enhance purification of plasmid DNA by non-ionic detergents. Biotechnol Bioeng 2011, 108:1872-1882. 10.1002/bit.23116, 3117116, 21351074.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1872-1882
    • Lezin, G.1    Kuehn, M.R.2    Brunelli, L.3
  • 29
    • 0024997246 scopus 로고
    • Removal of endotoxin from protein solutions by phase separation using Triton X-114
    • 10.1016/0022-1759(90)90029-U, 2170533
    • Aida Y, Pabst MJ. Removal of endotoxin from protein solutions by phase separation using Triton X-114. J Immunol Methods 1990, 132:191-195. 10.1016/0022-1759(90)90029-U, 2170533.
    • (1990) J Immunol Methods , vol.132 , pp. 191-195
    • Aida, Y.1    Pabst, M.J.2
  • 30
    • 84860799847 scopus 로고    scopus 로고
    • Optimization and efficient purification of recombinant Omp28 protein of Brucella melitensis using Triton X-100 and β-mercaptoethanol
    • 10.1016/j.pep.2012.04.002, 22542588
    • Kumar A, Tiwari S, Thavaselvam D, Sathyaseelan K, Prakash A, Barua A, Arora S, Kameswara Rao M. Optimization and efficient purification of recombinant Omp28 protein of Brucella melitensis using Triton X-100 and β-mercaptoethanol. Protein Expr Purif 2012, 83:226-232. 10.1016/j.pep.2012.04.002, 22542588.
    • (2012) Protein Expr Purif , vol.83 , pp. 226-232
    • Kumar, A.1    Tiwari, S.2    Thavaselvam, D.3    Sathyaseelan, K.4    Prakash, A.5    Barua, A.6    Arora, S.7    Kameswara Rao, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.