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Volumn 122, Issue 30, 2000, Pages 7402-7403

Chemically mediated site-specific cleavage of proteins [9]

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITY; BINDING SITE; CATALYSIS; LETTER; PROTEIN BINDING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS;

EID: 0034596319     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0002262     Document Type: Letter
Times cited : (13)

References (42)
  • 3
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    • Lactic acid (e.g., Fahnestock, S.; Rich, A. Science 1971, 173, 340) and glycolic acid (Chung, H.-H.; Benson, D. R.; Schultz, P. G. Science 1993, 259, 806) can be incorporated into proteins at discrete sites, affording baselabile ester bonds, but the derived protein analogues contain at least one linkage that can alter the stability and enzymatic activity of the protein (Chapman, E.; Thorson, J. S.; Schultz, P. G. J. Am. Chem. Soc. 1997, 119, 7151).
    • (1971) Science , vol.173 , pp. 340
    • Fahnestock, S.1    Rich, A.2
  • 4
    • 0027405662 scopus 로고
    • Lactic acid (e.g., Fahnestock, S.; Rich, A. Science 1971, 173, 340) and glycolic acid (Chung, H.-H.; Benson, D. R.; Schultz, P. G. Science 1993, 259, 806) can be incorporated into proteins at discrete sites, affording baselabile ester bonds, but the derived protein analogues contain at least one linkage that can alter the stability and enzymatic activity of the protein (Chapman, E.; Thorson, J. S.; Schultz, P. G. J. Am. Chem. Soc. 1997, 119, 7151).
    • (1993) Science , vol.259 , pp. 806
    • Chung, H.-H.1    Benson, D.R.2    Schultz, P.G.3
  • 5
    • 0030787794 scopus 로고    scopus 로고
    • Lactic acid (e.g., Fahnestock, S.; Rich, A. Science 1971, 173, 340) and glycolic acid (Chung, H.-H.; Benson, D. R.; Schultz, P. G. Science 1993, 259, 806) can be incorporated into proteins at discrete sites, affording baselabile ester bonds, but the derived protein analogues contain at least one linkage that can alter the stability and enzymatic activity of the protein (Chapman, E.; Thorson, J. S.; Schultz, P. G. J. Am. Chem. Soc. 1997, 119, 7151).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 7151
    • Chapman, E.1    Thorson, J.S.2    Schultz, P.G.3
  • 6
    • 85088074448 scopus 로고
    • A limited number of cleavage reagents have been reported; cleavage typically occurs at defined sequence but multiple sites (see, e.g.: (a) Lawson, W. B.; Gross, E.; Foltz, C. M.; Witkop, B. J. Am. Chem. Soc. 1961, 83, 1509. (b) Hotez, P. J.; Trang, N. L.; McKerrow, J. H.; Cerami, A. J. Biol. Chem. 1985, 260, 7343. Marcello, A.; Loregian, A.; De Filippis, V.; Fontana, A.; Hirst, T. R.; Palù, G. FEMS Microbiol. Lett. 1996, 136, 39).
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 1509
    • Lawson, W.B.1    Gross, E.2    Foltz, C.M.3    Witkop, B.4
  • 7
    • 0021831777 scopus 로고
    • A limited number of cleavage reagents have been reported; cleavage typically occurs at defined sequence but multiple sites (see, e.g.: (a) Lawson, W. B.; Gross, E.; Foltz, C. M.; Witkop, B. J. Am. Chem. Soc. 1961, 83, 1509. (b) Hotez, P. J.; Trang, N. L.; McKerrow, J. H.; Cerami, A. J. Biol. Chem. 1985, 260, 7343. Marcello, A.; Loregian, A.; De Filippis, V.; Fontana, A.; Hirst, T. R.; Palù, G. FEMS Microbiol. Lett. 1996, 136, 39).
    • (1985) J. Biol. Chem. , vol.260 , pp. 7343
    • Hotez, P.J.1    Trang, N.L.2    McKerrow, J.H.3    Cerami, A.4
  • 8
    • 0030042727 scopus 로고    scopus 로고
    • A limited number of cleavage reagents have been reported; cleavage typically occurs at defined sequence but multiple sites (see, e.g.: (a) Lawson, W. B.; Gross, E.; Foltz, C. M.; Witkop, B. J. Am. Chem. Soc. 1961, 83, 1509. (b) Hotez, P. J.; Trang, N. L.; McKerrow, J. H.; Cerami, A. J. Biol. Chem. 1985, 260, 7343. Marcello, A.; Loregian, A.; De Filippis, V.; Fontana, A.; Hirst, T. R.; Palù, G. FEMS Microbiol. Lett. 1996, 136, 39).
    • (1996) FEMS Microbiol. Lett. , vol.136 , pp. 39
    • Marcello, A.1    Loregian, A.2    De Filippis, V.3    Fontana, A.4    Hirst, T.R.5    Palù, G.6
  • 26
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    • Blakley, R. L., Benkovic, S. J., Eds.; Wiley: New York
    • (b) Johnson, L. F. In Folates and Pterins; Blakley, R. L., Benkovic, S. J., Eds.; Wiley: New York, 1984; Vol. 1, p 581.
    • (1984) Folates and Pterins , vol.1 , pp. 581
    • Johnson, L.F.1
  • 29
    • 0025946803 scopus 로고
    • AG in place of the wild-type activation peptide. A UAG codon was included at position -1, immediately prior to the authentic trypsin coding region. The hexahistidine moiety facilitated purification of the derived trypsinogen analogue on Ni-NTA agarose. (Janknecht, R.; de Martynoff, G.; Lou, J.; Hipskind, R. A.; Nordheim, A.; Stunnenberg, H. G. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 8972.)
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8972
    • Janknecht, R.1    De Martynoff, G.2    Lou, J.3    Hipskind, R.A.4    Nordheim, A.5    Stunnenberg, H.G.6
  • 33
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    • note
    • 5f
  • 34
    • 0343538221 scopus 로고    scopus 로고
    • note
    • 7a The ability of DHFR analogues to bind to Ni-NTA agarose and methotrexate-agarose was used to determine whether each analogue (i) contained a hexahistidine moiety at the N terminus and (ii) folded in a fashion similar to wild type, respectively.
  • 35
    • 0343538219 scopus 로고    scopus 로고
    • note
    • AGly at different positions (Table 1). Wild-type DHFR, and analogues Asp27Val and Glu-1Val gave no cleavage products under the same conditions (Table 1).
  • 36
    • 0343974039 scopus 로고    scopus 로고
    • note
    • 2 treatment afforded a protein that comigrated with an authentic standard by high-resolution PAGE and native capillary electrophoresis.
  • 37
    • 0343102304 scopus 로고    scopus 로고
    • note
    • The actual distances between the relevant carboxamide backbone residues and side chain carbon atoms determined crystallographically for DHFR support this interpretation (data not shown).


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