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max) of 454 nm. Typically, the stoichiometry of labeling is about 40 to 50 percent after correction for the presence of the second band in the LO preparation.
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0021191522
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K. A. Sullivan and H. M. Kagan, J. Biol. Chem. 257, 13520 (1982); H. Kuivaniemi, E. Savolainen, K. Kivirikko, ibid. 259, 6996 (1984); P. D. Burbelo, A. Monckeberg, C. O. Chichester, Collagen Relat Res. 6, 153 (1986).
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Kuivaniemi, H.1
Savolainen, E.2
Kivirikko, K.3
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37
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0022725289
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K. A. Sullivan and H. M. Kagan, J. Biol. Chem. 257, 13520 (1982); H. Kuivaniemi, E. Savolainen, K. Kivirikko, ibid. 259, 6996 (1984); P. D. Burbelo, A. Monckeberg, C. O. Chichester, Collagen Relat Res. 6, 153 (1986).
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Collagen Relat Res.
, vol.6
, pp. 153
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Burbelo, P.D.1
Monckeberg, A.2
Chichester, C.O.3
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38
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0027314128
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A. D. Cronshaw et al., Matrix 13, 255 (1993).
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(1993)
Matrix
, vol.13
, pp. 255
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Cronshaw, A.D.1
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39
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16044365477
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note
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3 (pH 8.0) containing 2 M urea at 3°C, with shaking. Proteolytic digestion was initiated by the addition of thermolysin to 4 percent (w/w). A second portion of the protease was added after 24 hours. The digestion was stopped after 49 hours by cooling the solution at - 70°C.
-
-
-
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40
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16044374331
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note
-
2O) with a linear gradient of 20 to 30 percent solvent B over 65 minutes at a flow rate of 1 ml per minute. Elution of peptides was monitored at 214 and 438 nm. The yield was 22 percent for the 36-minute peak based on radioactivity relative to that contained in the digestion solution.
-
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42
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16044368361
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note
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The predominant peak at 438 nm was lyophilized and redissolved in 50 mM sodium phosphate (pH 8.0). Subdigestion was initiated by the addition of Asp-N endoproteinase to a final concentration of 2.5 percent (w/w). The digestion mixture was incubated at 37°C with gentle shaking for 19 hours and later stored at - 7O°C. Peptides resulting from the digest were again separated on HPLC by a modification of a previously described procedure (5). A Vydac reversed-phase C18 column was used, and peptide elution was monitored at 220 and 438 nm. The single peak containing the active site peptide was collected, lyophilized, and subsequently used for sequencing, mass spectrometry, and resonance Raman studies. Overall yield for this single peak was about 26 percent relative to total peptides in the Asp-N digestion reaction. This corresponded to about 1.2 nmol of the active site peptide.
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44
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16044362773
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note
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Electrospray mass spectrum of the phenylhydrazine-derivatized LO active site peptide (sample 1) referred to as "basic structure" was acquired in an LC-ESIMS experiment with a Micromass BioQ quadrupole mass spectrometer equipped with an electrospray source. The mass spectrometer was scanned in noncontinuum mode over a range of m/z as 350 to 2000 at 5 s per scan.
-
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45
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0004124102
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A. L. Burlingame and S. A. Carr, Eds. Humana Press, Totowa, NJ, appendix XI
-
S. A. Carr and A. L. Burlingame, in Mass Spectrometry in the Biological Sciences, A. L. Burlingame and S. A. Carr, Eds. (Humana Press, Totowa, NJ, 1996), appendix XI, p. 546.
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(1996)
Mass Spectrometry in the Biological Sciences
, pp. 546
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Carr, S.A.1
Burlingame, A.L.2
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46
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16044374299
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note
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The accurate mass measurement was performed by Micromass AutoSpec SE spectrometry with etectrospray ionization on the triply charged ion of a cofactorcontaining peptide (sample 2) with doubly charged ions of bradykinin (m/z of 530.7885) and ceramicidin (m/z of 571.3608) as calibration standards.
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47
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0022466148
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P. R. Williamson, J. M. Kittler, J. W. Thanassi, H. M. Kagan, Biochem. J. 235, 597 (1986).
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(1986)
Biochem. J.
, vol.235
, pp. 597
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Williamson, P.R.1
Kittler, J.M.2
Thanassi, J.W.3
Kagan, H.M.4
-
50
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16044364703
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note
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The UV conditions were as follows: The phenylhydrazine derivative of LO protein was in 16 mM potassium phosphate (pH 7.8) containing 3.43 M urea; the phenylhydrazine derivative of LO model compound was in 100 mM potassium phosphate (pH 7.7) containing 3 M urea (30).
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53
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0028245290
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_, Biochemistry 33, 7647 (1994).
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(1994)
Biochemistry
, vol.33
, pp. 7647
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54
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0027965409
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R. Matsuzaki, T. Fukui, H. Sato, Y. Ozaki, K. Tanizawa, FEBS Lett. 351, 360 (1994); Y.-H. Choi et al., J. Biol. Chem. 270, 4712 (1995).
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FEBS Lett.
, vol.351
, pp. 360
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Matsuzaki, R.1
Fukui, T.2
Sato, H.3
Ozaki, Y.4
Tanizawa, K.5
-
55
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0028964417
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R. Matsuzaki, T. Fukui, H. Sato, Y. Ozaki, K. Tanizawa, FEBS Lett. 351, 360 (1994); Y.-H. Choi et al., J. Biol. Chem. 270, 4712 (1995).
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J. Biol. Chem.
, vol.270
, pp. 4712
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Choi, Y.-H.1
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56
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0029645871
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Ring flipping of TPQ has been confirmed by the crystal structure of the TPQ-containing amine oxidase from Escherichia coli [M. R. Parsons et al., Structure 3, 1171 (1995)].
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(1995)
Structure
, vol.3
, pp. 1171
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Parsons, M.R.1
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58
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0029080127
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M. Mure and J. P. Klinman, J. Am. Chem. Soc. 115, 7117 (1991); ibid. 117, 8707 (1995).
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(1995)
J. Am. Chem. Soc.
, vol.117
, pp. 8707
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59
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16044372452
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note
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2 M were incubated overnight in anhydrous acetonitrile. The reaction process was monitored by taking UV-Vis spectra at various reaction times. The final reaction mixture was examined by analytical HPLC.
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60
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0026426468
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K. Kenyon et al., Science 253, 802 (1991).
-
(1991)
Science
, vol.253
, pp. 802
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Kenyon, K.1
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61
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0011880118
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V. L. Davidson, Ed. Dekker, New York
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H. M. Kagan and P. C. Trackman, in Principles and Applications of Quinoproteins. V. L. Davidson, Ed. (Dekker, New York, 1993), pp. 173-189.
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(1993)
Principles and Applications of Quinoproteins
, pp. 173-189
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Kagan, H.M.1
Trackman, P.C.2
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62
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0027324732
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D. Bedell-Hogan, P. Trackman, W. Abrams, J. Rosenbloom, H. M. Kagan, J. Biol. Chem. 268, 10345 (1993).
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(1993)
J. Biol. Chem.
, vol.268
, pp. 10345
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Bedell-Hogan, D.1
Trackman, P.2
Abrams, W.3
Rosenbloom, J.4
Kagan, H.M.5
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64
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16044370120
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note
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Supported by NIH research grants GM39296 (J.P.K.), and GM27659 (D.M.D.), National Center for Research Resources Biomedical Research Technology Program grants P41 RR01614 (A.L.B.), and R37 AR 18880 and HL13262 (H.M.K.), and supported by the NSF Biological Instrumentation Program grant DIR 8700766 (A.L.B.).
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