Trehalose 6-phosphate synthase from Selaginella lepidophylla: purification and properties
Tipo de material:
TextoSeries ; BioChemical and Biophysical Research Communications, 313(2), p.314-319, 2004Trabajos contenidos: - Valenzuela-Soto, E.M
- Márquez-Escalante, J.A
- Iturriaga, G
- Figueroa-Soto, C.J
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A protein of 440 kDa with trehalose 6-phosphate synthase activity was purified with only one purification step by immobilized metal affinity chromatography, from fully hydrated Selaginella lepidophylla plants. The enzyme was purified 50-fold with a yield of 89
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