메뉴 건너뛰기




Volumn 249, Issue 2, 1997, Pages 505-509

Characterization of a stable intermediate trapped during reversible refolding of Bacillus subtilis α-amylase

Author keywords

Bacillus subtilis; Calcium folding effector; Folding and secretion; Folding intermediate; Amylase

Indexed keywords

AMYLASE;

EID: 0030691082     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00505.x     Document Type: Article
Times cited : (19)

References (18)
  • 1
    • 0023710642 scopus 로고
    • The molten globule state is involved in the transition of protein across membranes
    • Bychkova, V. E., Pain, R. H. & Ptitsyn, O. (1988) The molten globule state is involved in the transition of protein across membranes, FEBS Lett. 238, 231-234.
    • (1988) FEBS Lett. , vol.238 , pp. 231-234
    • Bychkova, V.E.1    Pain, R.H.2    Ptitsyn, O.3
  • 2
    • 0029004087 scopus 로고
    • Bacillus subtilis levansucrase: The efficiency of the second stage of secretion is modulated by external effectors assisting folding
    • Chambert, R., Haddaoui, E. & Petit-Glatron, M.-F. (1995) Bacillus subtilis levansucrase: the efficiency of the second stage of secretion is modulated by external effectors assisting folding, Microbiology 141, 997-1005.
    • (1995) Microbiology , vol.141 , pp. 997-1005
    • Chambert, R.1    Haddaoui, E.2    Petit-Glatron, M.-F.3
  • 3
    • 0023841559 scopus 로고
    • Protein unfolding and the energetics of protein translocation across biological membranes
    • Eilers, M. & Schatz, G. (1988) Protein unfolding and the energetics of protein translocation across biological membranes, Cell 52, 481-483.
    • (1988) Cell , vol.52 , pp. 481-483
    • Eilers, M.1    Schatz, G.2
  • 4
    • 0023656068 scopus 로고
    • Maintenance of intracellular calcium in Escherichia coli
    • Gangola, P. & Rosen, B. P. (1987) Maintenance of intracellular calcium in Escherichia coli, J. Biol. Chem. 262, 12 570-12 574.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12570-12574
    • Gangola, P.1    Rosen, B.P.2
  • 5
    • 0026759604 scopus 로고
    • Brominated phospholipids as a tool for monitoring the membrane insertion of colicin a
    • Gonzalez-Manas, J. M., Lakey, J. H. & Pattus, F. (1992) Brominated phospholipids as a tool for monitoring the membrane insertion of colicin A, Biochemistry 31, 7294-7300.
    • (1992) Biochemistry , vol.31 , pp. 7294-7300
    • Gonzalez-Manas, J.M.1    Lakey, J.H.2    Pattus, F.3
  • 6
    • 0029161085 scopus 로고
    • Characterization of a new cell-bound α-amylase in Bacillus subtilis 168 Marburg that is only immunologically related to the exocellular α-amylase
    • Haddaoui, E., Petit-Glatron, M.-F. & Chambert, R. (1995) Characterization of a new cell-bound α-amylase in Bacillus subtilis 168 Marburg that is only immunologically related to the exocellular α-amylase, J. Bacteriol. 177, 5158-5160.
    • (1995) J. Bacteriol. , vol.177 , pp. 5158-5160
    • Haddaoui, E.1    Petit-Glatron, M.-F.2    Chambert, R.3
  • 7
    • 0344524856 scopus 로고
    • α-Amylase formation and calcium metabolism of Bacillus subtilis
    • Hamada, N., Yamamoto, T. & Fukumoto, J. (1967) α-Amylase formation and calcium metabolism of Bacillus subtilis, Agr. Biol. Chem. 31, 1-6.
    • (1967) Agr. Biol. Chem. , vol.31 , pp. 1-6
    • Hamada, N.1    Yamamoto, T.2    Fukumoto, J.3
  • 8
    • 0029822373 scopus 로고    scopus 로고
    • Folding intermediates of a β barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism
    • Kleinschmidt, J. H. & Tamm, L. K. (1996) Folding intermediates of a β barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism, Biochemistry 35, 12 993-13 000.
    • (1996) Biochemistry , vol.35 , pp. 12993-13000
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 9
    • 0030831592 scopus 로고    scopus 로고
    • Characterization of the rate-limiting step of the secretion of Bacillus subtilis α-amylase overproduced during the exponential phase of growth
    • Leloup, L., Haddaoui, E., Chambert, R. & Petit-Glatron, M.-F. (1997) Characterization of the rate-limiting step of the secretion of Bacillus subtilis α-amylase overproduced during the exponential phase of growth, Microbiology 143, 3295-3303.
    • (1997) Microbiology , vol.143 , pp. 3295-3303
    • Leloup, L.1    Haddaoui, E.2    Chambert, R.3    Petit-Glatron, M.-F.4
  • 10
    • 0018719293 scopus 로고
    • Membrane bound and soluble extracellular α-amylase from Bacillus subtilis
    • Mäntsälä, P. & Zalkin, H. (1979) Membrane bound and soluble extracellular α-amylase from Bacillus subtilis, J. Biol. Chem. 254, 8540-8547.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8540-8547
    • Mäntsälä, P.1    Zalkin, H.2
  • 11
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis, J. Biochem. (Tokyo) 95, 511-519.
    • (1984) J. Biochem. (Tokyo) , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 12
    • 0026168310 scopus 로고
    • Pro-peptide as an intramolecular chaperone: Renaturation of denatured subtilisin e with a synthetic pro-peptide
    • Otha, Y., Hojo, H., Aimoto, S., Kobayaski, T., Zhu, X., Jordan, F. & Inouye, M. (1991) Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide. Mol. Microbiol. 5, 1507-1510.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1507-1510
    • Otha, Y.1    Hojo, H.2    Aimoto, S.3    Kobayaski, T.4    Zhu, X.5    Jordan, F.6    Inouye, M.7
  • 13
    • 0027297013 scopus 로고
    • The contribution of the cell wall to a transmembrane calcium gradient could play a key role in Bacillus subtilis protein secretion
    • Petit-Glatron, M.-F., Grajcar, L., Munz, A. & Chambert, R. (1993) The contribution of the cell wall to a transmembrane calcium gradient could play a key role in Bacillus subtilis protein secretion, Mol. Microbiol. 9, 1097-1106.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1097-1106
    • Petit-Glatron, M.-F.1    Grajcar, L.2    Munz, A.3    Chambert, R.4
  • 15
    • 0028826387 scopus 로고
    • Effect of folding on the export of ribosebinding protein studied with the genetically isolated suppressors for the signal sequence mutation
    • Song, T. & Park, C. (1995) Effect of folding on the export of ribosebinding protein studied with the genetically isolated suppressors for the signal sequence mutation, J. Mol. Biol. 253, 304-312.
    • (1995) J. Mol. Biol. , vol.253 , pp. 304-312
    • Song, T.1    Park, C.2
  • 16
    • 0026656792 scopus 로고
    • The molten globule intermediate for protein insertion or translocation through membranes
    • van der Goot, F. G., Lakey, J. H. & Pattus, F. (1992) The molten globule intermediate for protein insertion or translocation through membranes, Trends Cell Biol. 2, 343-348.
    • (1992) Trends Cell Biol. , vol.2 , pp. 343-348
    • Van Der Goot, F.G.1    Lakey, J.H.2    Pattus, F.3
  • 17
    • 0021111544 scopus 로고
    • Nucleotide sequence of the amylase gene from Bacillus subtilis
    • Yang, M., Galizzi, A. & Henner, D. (1983) Nucleotide sequence of the amylase gene from Bacillus subtilis, Nucleic Acids Res. 11, 237-249.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 237-249
    • Yang, M.1    Galizzi, A.2    Henner, D.3
  • 18
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., Wu, S. C. & Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism, Methods Enzymol. 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, S.C.2    Martinez, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.