By Nina Barbaresi
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Both Q2 and Q3 were operated in rf-only modes. Unit resolution was employed for all experiments. 8 ml/min. The orifice potential was set to 80 eV for the analysis of CNBr cleavage products and 100 eV for Factor Xa cleavage products. The electron multiplier was set at 3700 eV. IIL RESULTS AND DISCUSSION A. Rapid Desalting of Proteins We first investigated the capacity of perfusion packed capillary columns to rapidly purify high salt-containing proteins. Proteins submitted to our laboratory for mass spectral analysis are frequently solubilized in chaotropic agents, 8M urea or 6M GnHCl.
1991). Proceedings of the 39th Conference on Mass Spectrometry and Allied Topics, paper no. MP104, Nashville, TN, ASMS, East Lansing, MI. , and Yip, T-T. (1992). FEBS Letters 296, 99. , and Yip, T-T. (1991). J. Mol. Recog. 4, 151. W. (1992). Rapid Commun. Mass Spectrom. 6, 4. , Li, C M . , and Yip, T-T. (1992). J. Chromatogr. 604, 125. , Li, C M . , and Yip, T-T. (1992). Biol. Mass Spectrom. 21, 151. , Li, C M . W. (1992). The 40th American Society for Mass Spectrometry (ASMS) Conference on Mass Spectrometry and Allied Topics, Washington, DC, May 31-June 5.
In general, bacterial dihydrofolate reductases have a much higher affinity for the inhibitor trimethoprim than the mammalian enzymes, this difference in binding to the inhibitor is the basis for chemotherapeutic selectivity. MATERIALS AND METHODS Protein Purification. Human KL expressed in Exoli was purified in 8M urea/40 mM Tris-HCI, pH 7 on DEAE-Sepharose Fast Flow (Pharmacia, Uppsala, Sweden). After 100-fold dilution and dialysis against PBS followed by 40 mM TrisHCI, the protein was passed over Q-Sepharose Fast Flow (Pharmacia).