메뉴 건너뛰기




Volumn 22, Issue 10, 2011, Pages 2219-2229

Tryptophan complexed hydroxyapatite nanoparticles for immunoglobulin adsorption

Author keywords

[No Author keywords available]

Indexed keywords

AUTOIMMUNE DISEASE; DIFFERENTIAL SCANNING ANALYSIS; FOURIER TRANSFORM INFRARED; IS COSTS; MATRIX; MTT ASSAYS; NANO-SIZED HYDROXYAPATITE; POLYACRYLAMIDE GEL ELECTROPHORESIS; SELECTIVE REMOVAL; SYNERGIC EFFECTS; THERMAL GRAVIMETRIC ANALYSIS;

EID: 84855201831     PISSN: 09574530     EISSN: 15734838     Source Type: Journal    
DOI: 10.1007/s10856-011-4403-7     Document Type: Article
Times cited : (6)

References (38)
  • 2
    • 0034003927 scopus 로고    scopus 로고
    • Copper complexed polymer carriers for IgG adsorption
    • Hari PR, Paul W, Sharma CP. Copper complexed polymer carriers for IgG adsorption. J Biomed Mater Res. 2000;50:110-3.
    • (2000) J Biomed Mater Res. , vol.50 , pp. 110-3
    • Hari, P.R.1    Paul, W.2    Sharma, C.P.3
  • 3
    • 0029007779 scopus 로고
    • Elution of human IgG from affinity columns containing immobilised variants of protein A
    • Bottomley SP, Sutton BJ, Gore MG. Elution of human IgG from affinity columns containing immobilised variants of protein A. J Immunol Method. 1995;182:185-92.
    • (1995) J Immunol Method. , vol.182 , pp. 185-92
    • Bottomley, S.P.1    Sutton, B.J.2    Gore, M.G.3
  • 4
    • 0024543532 scopus 로고
    • Detection and reduction of Protein A contamination in immobilized Protein A purified monoclonal antibody preparations
    • DOI 10.1016/0022-1759(89)90121-X
    • Bloom JW, Wong MF, Mitra G. Detection and reduction of protein A contamination in immobilized protein A purified monoclonal antibody preparations. J Immunol Method. 1989;117: 83-9. (Pubitemid 19038721)
    • (1989) Journal of Immunological Methods , vol.117 , Issue.1 , pp. 83-89
    • Bloom, J.W.1    Wong, M.F.2    Mitra, G.3
  • 5
    • 0021728987 scopus 로고
    • Purification of monoclonal antibodies using high performance liquid chromatography (HPLC)
    • Perry GA, Jackson JD, McDonald TL, Crouse A, Sharp JG. Purification of monoclonal antibodies using high performance liquid chromatography (HPLC). Prep Biochem. 1984;14:431-7.
    • (1984) Prep Biochem. , vol.14 , pp. 431-7
    • Perry, G.A.1    Jackson, J.D.2    McDonald, T.L.3    Crouse, A.4    Sharp, J.G.5
  • 6
    • 0024620848 scopus 로고
    • Pseudobiospecific ligand affinity chromatography
    • Vijayalakshmi MA. Pseudobiospecific ligand affinity chromatography. Trends Biotechnol. 1989;l7:71-6.
    • (1989) Trends Biotechnol. , vol.17 , pp. 71-6
    • Vijayalakshmi, M.A.1
  • 8
    • 0029913144 scopus 로고    scopus 로고
    • Multiple-site binding interactions in metal-affinity chromatography
    • Johnson RD, Todd RJ, Arnold FH. Multiple-site binding interactions in metal-affinity chromatography. J Chromatogr A. 1996; 725:225-32.
    • (1996) J Chromatogr A , vol.725 , pp. 225-32
    • Johnson, R.D.1    Todd, R.J.2    Arnold, F.H.3
  • 9
    • 0034607361 scopus 로고    scopus 로고
    • Suitability of immobilized metal affinity chromatography for protein purification from canola
    • DOI 10.1002/(SICI)1097-0290(20000405)68:1<52::AID-BIT6>3.0.CO;2-A
    • Zhang CM, Reslewic SA, Glatz CE. Suitability of immobilized metal affinity chromatography for protein purification from canola. Biotechnol Bioeng. 2000;68:52-8. (Pubitemid 30163492)
    • (2000) Biotechnology and Bioengineering , vol.68 , Issue.1 , pp. 52-58
    • Zhang, C.-M.1    Reslewic, S.A.2    Glatz, C.E.3
  • 10
    • 0024306539 scopus 로고
    • Protein interactions with surfaceimmobilized metal ions: Structure-dependent variations in affinity and binding capacity with temperature and urea concentration
    • Yip TT, Nakagawa Y, Porath J. Protein interactions with surfaceimmobilized metal ions: Structure-dependent variations in affinity and binding capacity with temperature and urea concentration. J Anal Biochem. 1989;183:159-65.
    • (1989) J Anal Biochem. , vol.183 , pp. 159-65
    • Yip, T.T.1    Nakagawa, Y.2    Porath, J.3
  • 11
    • 0018824848 scopus 로고
    • Bioceramics consisting of calcium phosphate salts
    • DOI 10.1016/0142-9612(80)90059-9
    • Groot K. Bioceramics consisting of calcium phosphate salts. Biomaterials. 1980;1:47-50. (Pubitemid 10061158)
    • (1980) Biomaterials , vol.1 , Issue.1 , pp. 47-50
    • De Groot, K.1
  • 12
    • 33847805985 scopus 로고
    • Infrared studies of apatites
    • Fowler BO. Infrared studies of apatites. J Inorg Chem. 1974;13: 194-207.
    • (1974) J Inorg Chem. , vol.13 , pp. 194-207
    • Fowler, B.O.1
  • 13
    • 0346219399 scopus 로고    scopus 로고
    • Factorial screening of antibody purification processes using three chromatography steps without protein A
    • DOI 10.1016/j.chroma.2003.10.060
    • Deborah KF, Fahrner RL. Factorial screening of antibody purification processes using three chromatography steps without protein A. J Chromatogr A. 2004;1:79-85. (Pubitemid 37532537)
    • (2004) Journal of Chromatography A , vol.1024 , Issue.1-2 , pp. 79-85
    • Follman, D.K.1    Fahrner, R.L.2
  • 14
    • 0022325952 scopus 로고
    • Protein chromatography on hydroxyapatite columns
    • Gorbunoff MJ. Protein chromatography on hydroxyapatite columns. Methods Enzymol. 1985;117:370-80.
    • (1985) Methods Enzymol. , vol.117 , pp. 370-80
    • Gorbunoff, M.J.1
  • 15
    • 4344566963 scopus 로고    scopus 로고
    • Hydroxyapatite-based immobilized metal affinity adsorbents for protein purification
    • Suen RB, Lin SC, Hsu WH. Hydroxyapatite-based immobilized metal affinity adsorbents for protein purification. J Chromatogr A. 2004;1048:31-9.
    • (2004) J Chromatogr A. , vol.1048 , pp. 31-9
    • Suen, R.B.1    Lin, S.C.2    Hsu, W.H.3
  • 16
    • 1842863240 scopus 로고    scopus 로고
    • Chromatography on hydroxyapatite
    • Doonan S. Chromatography on hydroxyapatite. Methods Mol Biol. 2004;244:191-5.
    • (2004) Methods Mol Biol. , vol.244 , pp. 191-5
    • Doonan, S.1
  • 17
    • 0001631633 scopus 로고
    • Modified hydroxyapatite microspheres as immunoadsorbent for plasma perfusion
    • Paul W, Sharma CP. Modified hydroxyapatite microspheres as immunoadsorbent for plasma perfusion. J Colloid Interface Sci. 1995;174:224-9.
    • (1995) J Colloid Interface Sci. , vol.174 , pp. 224-9
    • Paul, W.1    Sharma, C.P.2
  • 19
    • 79955666018 scopus 로고    scopus 로고
    • Development and evaluation of cyclodextrin complexed hydroxyapatite nanoparticles for preferential albumin adsorption
    • Victor SP, Sharma CP. Development and evaluation of cyclodextrin complexed hydroxyapatite nanoparticles for preferential albumin adsorption. Colloids Surf B. 2011;85:221-8.
    • (2011) Colloids Surf B. , vol.85 , pp. 221-8
    • Victor, S.P.1    Sharma, C.P.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-5
    • Laemmli, U.K.1
  • 21
    • 0000221430 scopus 로고
    • Dependence of albumin-fibrinogen simple and competi- tive adsorption on surface properties of biomaterials
    • Brash JL, Uniyal S. Dependence of albumin-fibrinogen simple and competi- tive adsorption on surface properties of biomaterials. J Polym Sci Polym Symp. 1979;66:377-89.
    • (1979) J Polym Sci Polym Symp. , vol.66 , pp. 377-89
    • Brash, J.L.1    Uniyal, S.2
  • 22
    • 57349121969 scopus 로고    scopus 로고
    • Synthesis and characterization of PEGylated calcium phosphate nanoparticles for oral insulin delivery
    • Rukmani R, Paul W, Sharma CP. Synthesis and characterization of PEGylated calcium phosphate nanoparticles for oral insulin delivery. Biomed Mater Res B Appl Biomater. 2009;88:41-5.
    • (2009) Biomed Mater Res B Appl Biomater. , vol.88 , pp. 41-5
    • Rukmani, R.1    Paul, W.2    Sharma, C.P.3
  • 24
    • 34548024806 scopus 로고    scopus 로고
    • Loading and release studies of proteins using poly(N-isopropylacrylamide) based nanogels
    • Yan C, Elaissari A, Pichot C. Loading and release studies of proteins using poly(N-isopropylacrylamide) based nanogels. J Biomed Nanotechnol. 2006;2:208-16.
    • (2006) J Biomed Nanotechnol. , vol.2 , pp. 208-16
    • Yan, C.1    Elaissari, A.2    Pichot, C.3
  • 25
    • 0035387713 scopus 로고    scopus 로고
    • Adsorption of some essential amino acids on hydroxyapatite
    • DOI 10.1006/jcis.2001.7474
    • Shafei GMS, Moussa NA. Adsorption of some essential amino acids on hydroxyapatite. J Colloid Interface Sci. 2001;238:160-6. (Pubitemid 32896803)
    • (2001) Journal of Colloid and Interface Science , vol.238 , Issue.1 , pp. 160-166
    • El Shafei, G.M.S.1    Moussa, N.A.2
  • 26
    • 59049103834 scopus 로고    scopus 로고
    • Self-assembly of tryptophan-capped gold nanoparticles onto DNA network template
    • Sheikholeslami Z, Vosoughi M, Alemsadeh I. Self-assembly of tryptophan-capped gold nanoparticles onto DNA network template. J Dispers Sci Technol. 2009;30:255-9.
    • (2009) J Dispers Sci Technol. , vol.30 , pp. 255-9
    • Sheikholeslami, Z.1    Vosoughi, M.2    Alemsadeh, I.3
  • 27
    • 30744472423 scopus 로고    scopus 로고
    • Acclerated microwave processing of nanocrystalline hydroxyapatite
    • Ramesh Babu N, Prasad RK, Sampath Kumar TS. Acclerated microwave processing of nanocrystalline hydroxyapatite. J Mater Sci. 2005;40:6319-23.
    • (2005) J Mater Sci. , vol.40 , pp. 6319-23
    • Ramesh Babu, N.1    Prasad, R.K.2    Sampath Kumar, T.S.3
  • 28
    • 0037290523 scopus 로고    scopus 로고
    • FTIR, XRD, SEM and solid state NMR investigations of carbonate-containing hydroxyapatite nano-particles synthesized by hydroxide-gel technique
    • Panda RN, Hseich MF, Chung RJ, Chin TS. FTIR, XRD, SEM and solid state NMR investigations of carbonate-containing hydroxyapatite nano-particles synthesized by hydroxide-gel technique. J Phys Chem Solids. 2003;62:193-7.
    • (2003) J Phys Chem Solids. , vol.62 , pp. 193-7
    • Panda, R.N.1    Hseich, M.F.2    Chung, R.J.3    Chin, T.S.4
  • 29
    • 0037082714 scopus 로고    scopus 로고
    • Plasma protein adsorption pattern on characterized ceramic biomaterials
    • DOI 10.1016/S0142-9612(01)00244-7, PII S0142961201002447
    • Rosengren A, Pavlovic C, Oscarsson S, Krajewski A, Ravaglioli A, Piancastelli A. Plasma protein adsorption pattern on characterized ceramic biomaterials. Biomaterials. 2002;23:1237-47. (Pubitemid 33109056)
    • (2002) Biomaterials , vol.23 , Issue.4 , pp. 1237-1247
    • Rosengren, A.1    Pavlovic, E.2    Oscarsson, S.3    Krajewski, A.4    Ravaglioli, A.5    Piancastelli, A.6
  • 30
    • 0019079065 scopus 로고
    • Interaction of some serum proteins with hydroxyl apatite and other materials
    • Klein C, Ermiden PA, Van Kamp G. Interaction of some serum proteins with hydroxyl apatite and other materials. J Biomed Mater Res. 1980;14:705.
    • (1980) J Biomed Mater Res. , vol.14 , pp. 705
    • Klein, C.1    Ermiden, P.A.2    Van Kamp, G.3
  • 31
    • 0024830719 scopus 로고
    • Influence of steroid hormones on protein-platelet interaction at the blood-polymer interface
    • DOI 10.1016/0142-9612(89)90115-4
    • Sharma CP, Chandy T. Influence of steroid hormones on proteinplatelet interaction at the blood-polymer interface. Biomaterials. 1989;10:609-16. (Pubitemid 20021117)
    • (1989) Biomaterials , vol.10 , Issue.9 , pp. 609-616
    • Sharma, C.P.1    Chandy, T.2
  • 32
    • 0029973291 scopus 로고    scopus 로고
    • Tryptophan-immobilized column adsorbs immunoglobulin G anti-GQlb antibody from Fisher's syndrome
    • Yuki N. Tryptophan-immobilized column adsorbs immunoglobulin G anti-GQlb antibody from Fisher's syndrome. Neurology. 1996;46:1644-8.
    • (1996) Neurology , vol.46 , pp. 1644-8
    • Yuki, N.1
  • 34
    • 0026009271 scopus 로고
    • Adsorption and elution of bovine c-globulin using an affinity membrane containing hydrophobic amino acids as ligands
    • Kim M, Saito K, Furusaki Sato, Sugo T, Ishigaki T. Adsorption and elution of bovine c-globulin using an affinity membrane containing hydrophobic amino acids as ligands. J Chromatogr A. 1991;585:45-51.
    • (1991) J Chromatogr A , vol.585 , pp. 45-51
    • Kim, M.1    Saito, K.2    Sato, F.3    Sugo, T.4    Ishigaki, T.5
  • 35
    • 0024804921 scopus 로고
    • Comparison of immunoglobulin binding capacities and ligand leakage using eight different protein A affinity chromatography matrices
    • DOI 10.1016/0022-1759(89)90350-5
    • Fuglistaller P. Comparison of immunoglobulin binding capacities and ligand leakage using eight different protein A affinity chromography matrices. J Immunol Methods. 1989;124:171-7. (Pubitemid 20011349)
    • (1989) Journal of Immunological Methods , vol.124 , Issue.2 , pp. 171-177
    • Fuglistaller, P.1
  • 36
    • 0016717761 scopus 로고
    • Copper complexed polymer carriers for IgG adsorption
    • Porath J, Carlsson J, Olisson I, Belfrage G. Copper complexed polymer carriers for IgG adsorption. Nature. 1975;258:598-602.
    • (1975) Nature , vol.258 , pp. 598-602
    • Porath, J.1    Carlsson, J.2    Olisson, I.3    Belfrage, G.4
  • 37
    • 0026124797 scopus 로고
    • Adsorption of plasma proteins onto polymer lattice
    • Suzawa T, Shirahama H. Adsorption of plasma proteins onto polymer lattice. Adv Colloid Interface Sci. 1991;35:139-72.
    • (1991) Adv Colloid Interface Sci. , vol.35 , pp. 139-72
    • Suzawa, T.1    Shirahama, H.2
  • 38
    • 0034737392 scopus 로고    scopus 로고
    • Affinity chromatography on immobilized 'biomimetic' ligands: Synthesis, immobilization and chromatographic assessment of an immunoglobulin G-binding ligand
    • DOI 10.1016/S0378-4347(99)00549-6, PII S0378434799005496
    • Teng SF, Sproule K, Husain A, Lowe CR. Affinity chromatography on immobilized "biomimetic" ligands: synthesis, immobilization and chromatographic assessment of an immunoglobulin G-binding ligand. J Chromatogr B. 2000;740:1-15. (Pubitemid 30160867)
    • (2000) Journal of Chromatography B: Biomedical Sciences and Applications , vol.740 , Issue.1 , pp. 1-15
    • Teng, S.F.1    Sproule, K.2    Husain, A.3    Lowe, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.