메뉴 건너뛰기




Volumn 26, Issue 2, 2002, Pages 202-210

Production of recombinant endotoxin neutralizing protein in Pichia pastoris and methods for its purification

Author keywords

Endotoxin binding protein; LALF; Limulus; Pichia pastoris; Purification; rENP

Indexed keywords

LIMULUS; PICHIA; PICHIA PASTORIS; SYNTHETIC CONSTRUCT;

EID: 0036426424     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00508-9     Document Type: Article
Times cited : (12)

References (26)
  • 1
    • 0026760884 scopus 로고
    • Molecular mechanism of hemolymph clotting system in Limulus
    • S. Iwanaga, T. Miyata, F. Tokunaga, T. Muta, Molecular mechanism of hemolymph clotting system in Limulus, Thrombos. Res. 68 (1992) 1-32.
    • (1992) Thrombos. Res. , vol.68 , pp. 1-32
    • Iwanaga, S.1    Miyata, T.2    Tokunaga, F.3    Muta, T.4
  • 2
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • S. Iwanaga, S. Cebidae, T. Muta, New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions, J. Biochem. 123 (1998) 1-15.
    • (1998) J. Biochem. , vol.123 , pp. 1-15
    • Iwanaga, S.1    Cebidae, S.2    Muta, T.3
  • 3
    • 0021799698 scopus 로고
    • Isolation and biological activities of Limulus anticoagulant (Anti-LPS Factor) which interacts with lipopoly-saccharide (LPS)
    • T. Morita, S. Ohtsubo, T. Nakamura, S. Tanaka, S. Iwanaga, K. Ohashi, M. Niwa, Isolation and biological activities of Limulus anticoagulant (Anti-LPS Factor) which interacts with lipopoly-saccharide (LPS), J. Biochem. 97 (1985) 1611-1620.
    • (1985) J. Biochem. , vol.97 , pp. 1611-1620
    • Morita, T.1    Ohtsubo, S.2    Nakamura, T.3    Tanaka, S.4    Iwanaga, S.5    Ohashi, K.6    Niwa, M.7
  • 4
    • 0020416253 scopus 로고
    • Limulus anti-LPS factor: An anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system
    • S. Tanaka, T. Nakamura, T. Morita, S. Iwanaga, Limulus anti-LPS factor: An anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system, Biochem. Biophys. Res. Commun. 105 (1982) 717-723.
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 717-723
    • Tanaka, S.1    Nakamura, T.2    Morita, T.3    Iwanaga, S.4
  • 5
    • 0023352436 scopus 로고
    • Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus
    • T. Muta, T. Miyata, F. Tokunaga, R. Nakamura, S. Iwanaga, Primary structure of anti-lipopolysaccharide factor from Ameri-can horseshoe crab, Limulus polyphemus, J. Biochem. 101 (1987) 1321-1330.
    • (1987) J. Biochem. , vol.101 , pp. 1321-1330
    • Muta, T.1    Miyata, T.2    Tokunaga, F.3    Nakamura, R.4    Iwanaga, S.5
  • 6
    • 0023838558 scopus 로고
    • Enzymes required for yeast prohormone processing
    • S.R. Fuller, R.E. Sterne, J. Thorner, Enzymes required for yeast prohormone processing, Ann. Rev. Physiol. 50 (1988) 345-362.
    • (1988) Ann. Rev. Physiol. , vol.50 , pp. 345-362
    • Fuller, S.R.1    Sterne, R.E.2    Thorner, J.3
  • 7
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • J.M. Cregg, T.S. Vedrich, W.C. Rashke, Recent advances in the expression of foreign genes in Pichia pastoris, Biotechnology 11 (1993) 905-910.
    • (1993) Biotechnology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedrich, T.S.2    Rashke, W.C.3
  • 11
    • 14744271884 scopus 로고
    • High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene
    • J.J. Clare, F.B. Rayment, S.P. Ballantine, K. Sreekrishna, M.A. Ramanos, High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene, Biotechnology (NY) 9 (1991) 455-460.
    • (1991) Biotechnology (NY) , vol.9 , pp. 455-460
    • Clare, J.J.1    Rayment, F.B.2    Ballantine, S.P.3    Sreekrishna, K.4    Ramanos, M.A.5
  • 12
    • 0027171383 scopus 로고
    • Crystal structure of endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution
    • A. Hoess, S. Watson, G. Siber, R. Liddington, Crystal structure of endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution, EMBO J. 12 (1993) 3351-3356.
    • (1993) EMBO J. , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.3    Liddington, R.4
  • 15
    • 0011261249 scopus 로고
    • A. Nowotny, J.J. Spitzer, E.J. Ziegler (Eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, Elsevier, New York
    • J. Sambrook, E.F. Fritsch, T. Maniatis, in: A. Nowotny, J.J. Spitzer, E.J. Ziegler (Eds.), Molecular Cloning: A Laboratory Manual, Second Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, Elsevier, New York, 1989, pp. 315-325.
    • (1989) Molecular Cloning: A Laboratory Manual, Second Ed. , pp. 315-325
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 16
    • 0033919121 scopus 로고    scopus 로고
    • Reversible binding of heparin to the loop peptide of endotoxin neutralizing protein
    • R.J. Ridge, E.J. Paus, T.J. Novitsky, P.A. Ketchum, Reversible binding of heparin to the loop peptide of endotoxin neutralizing protein, J. Endotoxin. Res. 6 (2000) 17-23.
    • (2000) J. Endotoxin. Res. , vol.6 , pp. 17-23
    • Ridge, R.J.1    Paus, E.J.2    Novitsky, T.J.3    Ketchum, P.A.4
  • 17
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • A.D. Cardin, H.J.R. Weintraub, Molecular modeling of protein-glycosaminoglycan interactions, Arteriosclerosis 9 (1989) 21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.R.2
  • 18
    • 0031424642 scopus 로고    scopus 로고
    • High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties
    • T.R. Kim, Y. Goto, N. Hirota, K. Kuwata, H. Denton, S.Y. Wu, L. Sawyer, C.A. Batt, High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties, Protein Eng. 10 (1997) 1339-1345.
    • (1997) Protein Eng. , vol.10 , pp. 1339-1345
    • Kim, T.R.1    Goto, Y.2    Hirota, N.3    Kuwata, K.4    Denton, H.5    Wu, S.Y.6    Sawyer, L.7    Batt, C.A.8
  • 19
    • 0026094226 scopus 로고
    • Production of mouse epidermal growth factor in yeast: High-level secretion using Pichia pastoris strains containing multiple gene copies
    • J.J. Clare, M.A. Romanos, F.B. Rayment, J.E. Towedder, M.A. Smith, M.M. Payne, K. Sreekrishna, C.A. Henwood, Production of mouse epidermal growth factor in yeast: High-level secretion using Pichia pastoris strains containing multiple gene copies, Gene 105 (1991) 205-212.
    • (1991) Gene , vol.105 , pp. 205-212
    • Clare, J.J.1    Romanos, M.A.2    Rayment, F.B.3    Towedder, J.E.4    Smith, M.A.5    Payne, M.M.6    Sreekrishna, K.7    Henwood, C.A.8
  • 20
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • J.L. Creghino, J.M. Cregg, Heterologous protein expression in the methylotrophic yeast Pichia pastoris, FEMS Microbiol. Rev. 24 (2000) 45-66.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Creghino, J.L.1    Cregg, J.M.2
  • 21
    • 0034963608 scopus 로고    scopus 로고
    • Effect of copy number on the expression levels of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris
    • A. Vassileva, D. Arora Chugh, S. Swaminathan, N. Khanna, EJect of copy number on the expression levels of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris, Protein Expr. Purif. 21 (1) (2001) 71-80.
    • (2001) Protein Expr. Purif. , vol.21 , Issue.1 , pp. 71-80
    • Vassileva, A.1    Arora Chugh, D.2    Swaminathan, S.3    Khanna, N.4
  • 24
    • 0030903573 scopus 로고    scopus 로고
    • Glycosylation properties of the Pichia pastoris-expressed recombinant kringle 2 domain of tissue-type plasminogen activator
    • R.G. Miele, S.L. Nilsen, T. Brito, R.K. Bretthauer, F.J. Castel-lino, Glycosylation properties of the Pichia pastoris-expressed recombinant kringle 2 domain of tissue-type plasminogen activator, Biotechnol. Appl. Biochem. 25 part 2 (1997) 151-157.
    • (1997) Biotechnol. Appl. Biochem. , vol.25 , Issue.PART 2 , pp. 151-157
    • Miele, R.G.1    Nilsen, S.L.2    Brito, T.3    Bretthauer, R.K.4    Castellino, F.J.5
  • 25
    • 0034053424 scopus 로고    scopus 로고
    • Characterization of glycosylated streptokinase secreted from Pichia pastoris: Enhanced resistance of SK to proteolysis by glycosylation
    • J. Pratap, G. Rajamohan, K.L. Dikshit, Characterization of glycosylated streptokinase secreted from Pichia pastoris: Enhanced resistance of SK to proteolysis by glycosylation, Appl. Microbiol. Biotechnol. 53 (2000) 469-475.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 469-475
    • Pratap, J.1    Rajamohan, G.2    Dikshit, K.L.3
  • 26
    • 0033777689 scopus 로고    scopus 로고
    • Glycosylation of prourokinase produced by Pichia pastoris impairs enzymatic activity but not secretion
    • P. Wang, J. Zhang, Z. Sun, Y. Chen, J.N. Liu, Glycosylation of prourokinase produced by Pichia pastoris impairs enzymatic activity but not secretion, Protein Expr. Purif. 20 (2000) 179-185.
    • (2000) Protein Expr. Purif. , vol.20 , pp. 179-185
    • Wang, P.1    Zhang, J.2    Sun, Z.3    Chen, Y.4    Liu, J.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.