메뉴 건너뛰기




Volumn 4, Issue 9, 2009, Pages 1345-1356

Tandem multimer expression of angiotensin I-converting enzyme inhibitory peptide in Escherichia coli

Author keywords

Anti peptide antibody; Inclusion bodies; Multimer; Recombinant tandem peptide; Restriction enzyme

Indexed keywords

ANTI-PEPTIDE ANTIBODY; INCLUSION BODIES; MULTIMER; RECOMBINANT TANDEM PEPTIDE; RESTRICTION ENZYME;

EID: 70350090610     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.200800326     Document Type: Article
Times cited : (14)

References (33)
  • 1
    • 0014957830 scopus 로고
    • A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin
    • Yang, H. Y. T., Erdos, E. G., Levin, Y., A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim. Biophys. Acta 1970, 214, 374-376.
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 374-376
    • Yang, H.Y.T.1    Erdos, E.G.2    Levin, Y.3
  • 2
    • 0025101603 scopus 로고
    • Angiotensin converting enzyme inhibition and its impact on cardiovascular disease
    • Gavras, H., Angiotensin converting enzyme inhibition and its impact on cardiovascular disease. Circulation 1990, 81, 381-388.
    • (1990) Circulation , vol.81 , pp. 381-388
    • Gavras, H.1
  • 3
    • 32244435191 scopus 로고    scopus 로고
    • Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice
    • Hasan, M. F., Kitagawa, M., Kumada,Y., Hashimoto, N. et al., Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice. Process. Biochem. 2006, 41, 505-511.
    • (2006) Process. Biochem , vol.41 , pp. 505-511
    • Hasan, M.F.1    Kitagawa, M.2    Kumada, Y.3    Hashimoto, N.4
  • 4
    • 0023811008 scopus 로고
    • Isolation of angiotensin-converting enzyme inhibitor from tuna muscle
    • Kohama,Y., Matsumoto, S., Oka H., Teramoto, T. et al., Isolation of angiotensin-converting enzyme inhibitor from tuna muscle. Biochem. Biophys. Res. Commun. 1988, 155, 332-337.
    • (1988) Biochem. Biophys. Res. Commun , vol.155 , pp. 332-337
    • Kohama, Y.1    Matsumoto, S.2    Oka, H.3    Teramoto, T.4
  • 5
    • 0025928822 scopus 로고
    • Purification of secreted recombinant proteins from Escherichia coli
    • Le, H. V., Trotta, P. P., Purification of secreted recombinant proteins from Escherichia coli. Bioprocess Technol. 1991, 12, 163-181.
    • (1991) Bioprocess Technol , vol.12 , pp. 163-181
    • Le, H.V.1    Trotta, P.P.2
  • 6
    • 0032877184 scopus 로고    scopus 로고
    • Therapeutic peptides revisited
    • Latham, P.W., Therapeutic peptides revisited. Nat. Biotechnol. 1999, 17, 755-757.
    • (1999) Nat. Biotechnol , vol.17 , pp. 755-757
    • Latham, P.W.1
  • 7
    • 0034054551 scopus 로고    scopus 로고
    • Construction and expression of functional multi-domain polypeptides in Escherichia coli: Expression of the Neurospora crassa metallothionein gene
    • Mauro, J. M., Pazirandeh, M., Construction and expression of functional multi-domain polypeptides in Escherichia coli: expression of the Neurospora crassa metallothionein gene. Lett. Appl. Microbiol. 2000, 2, 161-166.
    • (2000) Lett. Appl. Microbiol , vol.2 , pp. 161-166
    • Mauro, J.M.1    Pazirandeh, M.2
  • 8
    • 0032484702 scopus 로고    scopus 로고
    • Recombinant production and purification of novel antimicrobial peptide in Escherichia coli
    • Haught, C. D., Subramanian, G. D., Jackson, R. K.W., Harrison, R.G., Recombinant production and purification of novel antimicrobial peptide in Escherichia coli. Biotechnol. Bioeng. 1998, 57, 55-61.
    • (1998) Biotechnol. Bioeng , vol.57 , pp. 55-61
    • Haught, C.D.1    Subramanian, G.D.2    Jackson, R.K.W.3    Harrison, R.G.4
  • 9
    • 14744289727 scopus 로고
    • Renaturation of a singlechain immunotoxin facilitated by chaperones and protein disul-fide isomerase
    • Buchner, J., Brinkmann,U., Pastan, I., Renaturation of a singlechain immunotoxin facilitated by chaperones and protein disul-fide isomerase. Biotechnology (NY) 1992, 10, 682-685.
    • (1992) Biotechnology (NY) , vol.10 , pp. 682-685
    • Buchner, J.1    Brinkmann, U.2    Pastan, I.3
  • 10
    • 0031828229 scopus 로고    scopus 로고
    • High-level expression of the angiotensin-converting-enzyme-inhibiting peptide, YG-1, as tandem multimers in Escherichia coli
    • Park, C. J., Lee, J. H., Hong, S. S., Lee, H. S. et al., High-level expression of the angiotensin-converting-enzyme-inhibiting peptide, YG-1, as tandem multimers in Escherichia coli. Appl. Microbiol. Biotechnol. 1998, 50, 71-76.
    • (1998) Appl. Microbiol. Biotechnol , vol.50 , pp. 71-76
    • Park, C.J.1    Lee, J.H.2    Hong, S.S.3    Lee, H.S.4
  • 11
    • 36749044744 scopus 로고    scopus 로고
    • pro fusion technology to produce proteins with authentic N termini in E. coli
    • pro fusion technology to produce proteins with authentic N termini in E. coli. Nat. Methods 2007, 12, 1037-1043.
    • (2007) Nat. Methods , vol.12 , pp. 1037-1043
    • Achmüller, C.1    Kaar, W.2    Ahrer, K.3    Wechner, P.4
  • 12
    • 0033083510 scopus 로고    scopus 로고
    • Design and expression of a synthetic mucin gene fragment in Escherichia Coli
    • Dolby, N., Dombrowski, K. E., Wright, S. E., Design and expression of a synthetic mucin gene fragment in Escherichia Coli. Protein Expression and Purification 1999, 15, 146-154.
    • (1999) Protein Expression and Purification , vol.15 , pp. 146-154
    • Dolby, N.1    Dombrowski, K.E.2    Wright, S.E.3
  • 13
    • 0030500402 scopus 로고    scopus 로고
    • Sequential amplification of cloned DNA as tandem multimers using class-IIS restriction enzymes
    • Lee, J. H., Skowron, P. M., Rutkowska, S. M., Hong, S. S. et al., Sequential amplification of cloned DNA as tandem multimers using class-IIS restriction enzymes. Genetic Analysis: Biomol. Eng. 1996, 13, 139-145.
    • (1996) Genetic Analysis: Biomol. Eng , vol.13 , pp. 139-145
    • Lee, J.H.1    Skowron, P.M.2    Rutkowska, S.M.3    Hong, S.S.4
  • 14
    • 0141705727 scopus 로고    scopus 로고
    • Changgui, L., Patricia, Ng M. L., Zhu, Y.,Ho, B. et al., Tandem repeats of Sushi3 peptide with enhanced LPS-binding and -neutralizing activities. Protein Eng. 2003, 16, 629-635.
    • Changgui, L., Patricia, Ng M. L., Zhu, Y.,Ho, B. et al., Tandem repeats of Sushi3 peptide with enhanced LPS-binding and -neutralizing activities. Protein Eng. 2003, 16, 629-635.
  • 15
    • 0034724941 scopus 로고    scopus 로고
    • Production of antifungal recombinant peptides in Escherichia coli
    • Gavit, P., Better, M., Production of antifungal recombinant peptides in Escherichia coli. J. Biotechnol. 2000, 79, 127-136.
    • (2000) J. Biotechnol , vol.79 , pp. 127-136
    • Gavit, P.1    Better, M.2
  • 16
    • 0036207353 scopus 로고    scopus 로고
    • Expression and purification of an ACE-inhibitory peptide multimer from synthetic DNA in Escherichia coli
    • Kwang-Seok, O., Yong-Sung, P., HA-Chin, S., Expression and purification of an ACE-inhibitory peptide multimer from synthetic DNA in Escherichia coli. J. Microbiol. Biotechnol. 2002, 12, 59-64.
    • (2002) J. Microbiol. Biotechnol , vol.12 , pp. 59-64
    • Kwang-Seok, O.1    Yong-Sung, P.2    HA-Chin, S.3
  • 17
    • 0037358662 scopus 로고    scopus 로고
    • Overexpression and purification of recombinant atrial natriuretic peptide using hybrid fusion protein REF-ANP in Escherichia coli
    • Wang, J., Chen, W., Lu, J., Lu, S., Overexpression and purification of recombinant atrial natriuretic peptide using hybrid fusion protein REF-ANP in Escherichia coli. Protein Expression and Purification 2003, 28, 49-56.
    • (2003) Protein Expression and Purification , vol.28 , pp. 49-56
    • Wang, J.1    Chen, W.2    Lu, J.3    Lu, S.4
  • 18
    • 36448980664 scopus 로고    scopus 로고
    • Production of active angiotensin-I converting enzyme inhibitory peptides derived from bovine β-casein by recombinant DNA technologies
    • Losacco, M., Gallerani, R., Gobbetti, M., Minervini, F. et al., Production of active angiotensin-I converting enzyme inhibitory peptides derived from bovine β-casein by recombinant DNA technologies. Biotechnol. J. 2007, 2, 1425-1434.
    • (2007) Biotechnol. J , vol.2 , pp. 1425-1434
    • Losacco, M.1    Gallerani, R.2    Gobbetti, M.3    Minervini, F.4
  • 19
    • 34447310561 scopus 로고    scopus 로고
    • High-level expression of milk-derived antihypertensive peptide in Escherichia coli and its bioactivity
    • Liu, D., Sun, H., Zhang, L., Li, Z. et al., High-level expression of milk-derived antihypertensive peptide in Escherichia coli and its bioactivity. J. Agric. Food Chem. 2007, 55, 5109-5112.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 5109-5112
    • Liu, D.1    Sun, H.2    Zhang, L.3    Li, Z.4
  • 21
    • 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
  • 22
    • 0022652364 scopus 로고
    • A general method for retrieving the components of a genetically engineered fusion protein
    • Szoka, P. R., Achreiber, A. B., Chan, H., Murthy, J., A general method for retrieving the components of a genetically engineered fusion protein. DNA 1986, 5, 11-20.
    • (1986) DNA , vol.5 , pp. 11-20
    • Szoka, P.R.1    Achreiber, A.B.2    Chan, H.3    Murthy, J.4
  • 23
    • 34547542456 scopus 로고    scopus 로고
    • Screening of ACE-inhibitory peptides from a random peptide-displayed phage library using ACE-coupled liposomes
    • Kumada, Y., Hashimoto, N., Hasan, F., Terashima, M. et al., Screening of ACE-inhibitory peptides from a random peptide-displayed phage library using ACE-coupled liposomes. J. Biotechnol. 2007, 131, 144-149.
    • (2007) J. Biotechnol , vol.131 , pp. 144-149
    • Kumada, Y.1    Hashimoto, N.2    Hasan, F.3    Terashima, M.4
  • 24
    • 33746294478 scopus 로고    scopus 로고
    • Molecular cloning of protein-based polymers
    • Mi, L., Molecular cloning of protein-based polymers. Biomacromolecules 2006, 7, 2099-2107.
    • (2006) Biomacromolecules , vol.7 , pp. 2099-2107
    • Mi, L.1
  • 25
    • 0035907064 scopus 로고    scopus 로고
    • Design and production of genetically modified soybean protein with anti-hypertensive activity by incorporating potent analogue of ovokinin (2-7)
    • Matoba, N., Doyama, N., Yamada, Y., Maruyama, N. et al., Design and production of genetically modified soybean protein with anti-hypertensive activity by incorporating potent analogue of ovokinin (2-7). FEBS Lett. 2001, 497, 50-54.
    • (2001) FEBS Lett , vol.497 , pp. 50-54
    • Matoba, N.1    Doyama, N.2    Yamada, Y.3    Maruyama, N.4
  • 26
    • 1542284546 scopus 로고    scopus 로고
    • Optimal designing of β-conglycinin to genetically incorporate RPLKPW, a potent anti-hypertensive peptide
    • Onishi, K., Matoba, N., Yamada, Y., Doyama, N. et al., Optimal designing of β-conglycinin to genetically incorporate RPLKPW, a potent anti-hypertensive peptide. Peptides 2004, 25, 37-43.
    • (2004) Peptides , vol.25 , pp. 37-43
    • Onishi, K.1    Matoba, N.2    Yamada, Y.3    Doyama, N.4
  • 27
    • 20144389321 scopus 로고    scopus 로고
    • Design and expression of peptide antibiotic hPAB-b as tandem multimers in Escherichia coli
    • Rao, X., Hu, J., Li, S., Jin, X. et al., Design and expression of peptide antibiotic hPAB-b as tandem multimers in Escherichia coli. Peptides 2005, 26, 721-729.
    • (2005) Peptides , vol.26 , pp. 721-729
    • Rao, X.1    Hu, J.2    Li, S.3    Jin, X.4
  • 28
    • 33745553939 scopus 로고    scopus 로고
    • Fragmentation of angiotensin-I converting enzyme inhibitory peptides from bonito meat under intestinal digestion conditions and their characterization
    • Hasan, M. F., Kumada, Y., Hashimoto, N., Katsuda, T. et al., Fragmentation of angiotensin-I converting enzyme inhibitory peptides from bonito meat under intestinal digestion conditions and their characterization. Food Bioproducts Process. 2006, 84, 135-138.
    • (2006) Food Bioproducts Process , vol.84 , pp. 135-138
    • Hasan, M.F.1    Kumada, Y.2    Hashimoto, N.3    Katsuda, T.4
  • 29
    • 0141575314 scopus 로고    scopus 로고
    • Expression of milk derived antihypertensive peptides in Escherichia coli
    • Lv, G.S., Huo, G.C., Fu, X.Y., Expression of milk derived antihypertensive peptides in Escherichia coli. J. Dairy Sci. 2003, 86, 1927-1931.
    • (2003) J. Dairy Sci , vol.86 , pp. 1927-1931
    • Lv, G.S.1    Huo, G.C.2    Fu, X.Y.3
  • 30
    • 34547471587 scopus 로고    scopus 로고
    • Expression of antihypertensive peptide, His-His-Leu, as tandem repeats in Escherichia coli
    • Do-Won, J., Shin, D. S., Ahan C-W., Song, I. S., Expression of antihypertensive peptide, His-His-Leu, as tandem repeats in Escherichia coli. J. Microbiol. Biotechnol. 2007, 17, 952-959.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 952-959
    • Do-Won, J.1    Shin, D.S.2    Ahan, C.-W.3    Song, I.S.4
  • 31
    • 33846518778 scopus 로고    scopus 로고
    • ACE inhibitory activity and characteristics of tri-peptides obtained from bonito protein
    • Hasan, M.F., Kobayashi, Y., Kumada, Y., Katsuda, T. et al., ACE inhibitory activity and characteristics of tri-peptides obtained from bonito protein. J. Chem. Eng. Jpn. 2007, 40, 59-62.
    • (2007) J. Chem. Eng. Jpn , vol.40 , pp. 59-62
    • Hasan, M.F.1    Kobayashi, Y.2    Kumada, Y.3    Katsuda, T.4
  • 32
    • 0033860508 scopus 로고    scopus 로고
    • Classification and antihypertensive activity of angiotensin-I converting enzyme inhibitory peptides derived from food proteins
    • Fujita, H., Yokoyama, K., Yoshikawa, M., Classification and antihypertensive activity of angiotensin-I converting enzyme inhibitory peptides derived from food proteins. J. Food. Sci. 2000, 65, 4564-4569.
    • (2000) J. Food. Sci , vol.65 , pp. 4564-4569
    • Fujita, H.1    Yokoyama, K.2    Yoshikawa, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.