Abstract
Soybean urease has been purified 76.51 fold by the use of the DEAE-Sepharose CL-6B column chromatography technique. The purified enzyme was applied to the SDS-PAGE electrophoresis. The effect on Ni ions to the enzyme was tested. Activation determinations were carried out by the Nesslerization method detecting the ammonia content at 425 nm, the protein content was detected by the Warburg and Christian method.
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