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Volumn 66, Issue 1, 2000, Pages 304-309

Efficient production of artificially designed gelatins with a Bacillus brevis system

Author keywords

[No Author keywords available]

Indexed keywords

GELATIN;

EID: 0033989390     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.1.304-309.2000     Document Type: Article
Times cited : (21)

References (17)
  • 1
    • 0042547980 scopus 로고
    • Synthetic polypeptide models of collagen: Synthesis and applications
    • G. N. Ramachandran and A. H. Reddi (ed.), Plenum Press, New York, N. Y.
    • Bhatnagar, R. S., and R. S. Rapaka. 1976. Synthetic polypeptide models of collagen: synthesis and applications, p. 479-523. In G. N. Ramachandran and A. H. Reddi (ed.), Biochemistry of collagen. Plenum Press, New York, N. Y.
    • (1976) Biochemistry of Collagen , pp. 479-523
    • Bhatnagar, R.S.1    Rapaka, R.S.2
  • 3
    • 0013541377 scopus 로고
    • High-voltage paper electrophoresis
    • Dreyer, W., and E. Bynum. 1967. High-voltage paper electrophoresis. Methods Enzymol. 11:32-39.
    • (1967) Methods Enzymol. , vol.11 , pp. 32-39
    • Dreyer, W.1    Bynum, E.2
  • 4
    • 0024467132 scopus 로고
    • Cloning and expression of a collagen-analog-encoding synthetic gene in Escherichia coli
    • Goldberg, I., A. J. Salerno, T. Patterson, and J. I. Williams. 1989. Cloning and expression of a collagen-analog-encoding synthetic gene in Escherichia coli. Gene 80:305-314.
    • (1989) Gene , vol.80 , pp. 305-314
    • Goldberg, I.1    Salerno, A.J.2    Patterson, T.3    Williams, J.I.4
  • 5
    • 0018887210 scopus 로고
    • The anomalous behavior of collagen peptides on sodium dodecyl sulfate-polyacrylamide gel electrophoresis is due to the low content of hydrophobic amino acid residues
    • Hayashi, T., and Y. Nagai. 1980. The anomalous behavior of collagen peptides on sodium dodecyl sulfate-polyacrylamide gel electrophoresis is due to the low content of hydrophobic amino acid residues. J. Biochem. 87:803-808.
    • (1980) J. Biochem. , vol.87 , pp. 803-808
    • Hayashi, T.1    Nagai, Y.2
  • 6
    • 0031899035 scopus 로고    scopus 로고
    • Artificial fibrous proteins
    • Heslot, H. 1998. Artificial fibrous proteins. Biochimie 80:19-31.
    • (1998) Biochimie , vol.80 , pp. 19-31
    • Heslot, H.1
  • 7
    • 0032929259 scopus 로고    scopus 로고
    • Isolation of a protease-deficient mutant of Bacillus brevis and efficient secretion of a fungal protein disulfide isomerase by the mutant
    • Kajino, T., K. Kato, C. Miyazaki, O. Asami, Y. Yamada, M. Hirai, and S. Udaka. 1999. Isolation of a protease-deficient mutant of Bacillus brevis and efficient secretion of a fungal protein disulfide isomerase by the mutant. J. Biosci. Bioeng. 87:37-42.
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 37-42
    • Kajino, T.1    Kato, K.2    Miyazaki, C.3    Asami, O.4    Yamada, Y.5    Hirai, M.6    Udaka, S.7
  • 8
    • 0031464905 scopus 로고    scopus 로고
    • Extracellular production of an intact and biologically active human growth hormone by the Bacillus brevis system
    • Kajino, T., Y. Saito, M. Hirai, O. Asami, Y. Yamada, and S. Udaka. 1998. Extracellular production of an intact and biologically active human growth hormone by the Bacillus brevis system. J. Ind. Microbiol. Biotechnol. 19:227-231.
    • (1998) J. Ind. Microbiol. Biotechnol. , vol.19 , pp. 227-231
    • Kajino, T.1    Saito, Y.2    Hirai, M.3    Asami, O.4    Yamada, Y.5    Udaka, S.6
  • 9
    • 0029411534 scopus 로고
    • Efficient production of Casoxin D, a bradykinin agonist peptide derived from human casein, by Bacillus brevis
    • Kato, M., Y. Fujiwara, A. Okamoto, M. Yoshikawa, H. Chiba, and S. Udaka. 1995. Efficient production of Casoxin D, a bradykinin agonist peptide derived from human casein, by Bacillus brevis. Biosci. Biotechnol. Biochem. 59:2056-2059.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 2056-2059
    • Kato, M.1    Fujiwara, Y.2    Okamoto, A.3    Yoshikawa, M.4    Chiba, H.5    Udaka, S.6
  • 10
    • 0030174911 scopus 로고    scopus 로고
    • Expression and purification of a spider silk protein: A new strategy for producing repetitive proteins
    • Lewis, R. V., M. Hinman. S. Kothakota, and M. J. Fournier. 1996. Expression and purification of a spider silk protein: a new strategy for producing repetitive proteins. Protein Expr. Purif. 7:400-406.
    • (1996) Protein Expr. Purif. , vol.7 , pp. 400-406
    • Lewis, R.V.1    Hinman, M.2    Kothakota, S.3    Fournier, M.J.4
  • 11
    • 0028945002 scopus 로고
    • Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin
    • Martin, S. L., B. Vrhovski, and A. S. Weiss. 1995. Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin. Gene 154:159-166.
    • (1995) Gene , vol.154 , pp. 159-166
    • Martin, S.L.1    Vrhovski, B.2    Weiss, A.S.3
  • 13
    • 0015862613 scopus 로고
    • Hydroxyproline content determines the denaturation temperature of chick tendon collagen
    • Rosenbloom, J., M. Harsch, and S. A. Jimenez. 1973. Hydroxyproline content determines the denaturation temperature of chick tendon collagen. Arch. Biochem. Biophys. 158:478-481.
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 478-481
    • Rosenbloom, J.1    Harsch, M.2    Jimenez, S.A.3
  • 14
    • 0027985475 scopus 로고
    • Direct high-level secretion into the culture medium of tuna growth hormone in biologically active form by Bacillus brevis
    • Sagiya, Y., H. Yamagata, and S. Udaka. 1994. Direct high-level secretion into the culture medium of tuna growth hormone in biologically active form by Bacillus brevis. Appl. Microbiol. Biotechnol. 42:358-363.
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 358-363
    • Sagiya, Y.1    Yamagata, H.2    Udaka, S.3
  • 15
    • 0031264633 scopus 로고    scopus 로고
    • Secretion of human interleukin-2 in biologically active form by Bacillus brevis directly into culture medium
    • Takimura, Y., M. Kato, T. Ohta, H. Yamagata, and S. Udaka. 1997. Secretion of human interleukin-2 in biologically active form by Bacillus brevis directly into culture medium. Biosci. Biotechnol. Biochem. 61:1858-1861.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1858-1861
    • Takimura, Y.1    Kato, M.2    Ohta, T.3    Yamagata, H.4    Udaka, S.5
  • 16
    • 0023959447 scopus 로고
    • Characterization of the genes for the hexagonally arranged surface layer proteins in protein-producing Bacillus brevis 47: Complete nucleotide sequence of the middle wall protein gene
    • Tsuboi, A., R. Uchihi, T. Adachi, T. Sasaki, S. Hayakawa, H. Yamagata, N. Tsukagoshi, and S. Udaka. 1988. Characterization of the genes for the hexagonally arranged surface layer proteins in protein-producing Bacillus brevis 47: complete nucleotide sequence of the middle wall protein gene. J. Bacteriol. 170:935-945.
    • (1988) J. Bacteriol. , vol.170 , pp. 935-945
    • Tsuboi, A.1    Uchihi, R.2    Adachi, T.3    Sasaki, T.4    Hayakawa, S.5    Yamagata, H.6    Tsukagoshi, N.7    Udaka, S.8
  • 17
    • 0027297667 scopus 로고
    • High-level secretion of heterologous proteins by Bacillus brevis
    • Udaka, S., and H. Yamagata. 1993. High-level secretion of heterologous proteins by Bacillus brevis. Methods Enzymol. 217:23-33.
    • (1993) Methods Enzymol. , vol.217 , pp. 23-33
    • Udaka, S.1    Yamagata, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.