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Figure 1
(a) Heparin affinity chromatography of tCid1 (without GST fused). The co-purified nucleic acids bound to the tCid1 enzyme (and mutants) were displaced by heparin affinity chromatography of tCid1. The protein that bound to the immobilized heparin was eluted using a linear sodium chloride gradient from 50 to 2 M. A single symmetrical peak eluted as a result of the sodium chloride gradient and clearly displays a significant absorbance at 280 nm and a greatly reduced 260:280 nm absorbance ratio. (b) SDS–PAGE analysis of the protein composition of the two peaks.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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