Abstract
The Ribulose-1,5-bisphosphafe-carboxylase (RuBPcase) has been purified to electrophoretic homogeneity from jerusalem artichoke ( Helianthus tuberosus L. ) by an original laboratory method. The molecular properties of the purified active enzyme in solution are reported. The molecular characteristics and the specific enzyme activity have been used to test the final preparation of RuBPcase from jerusalem artichoke by the typical wet green crop fractionation procedure.
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