A new procedure for the purification of spinach leaf photosynthetic fructose-1,6-bisphosphatase by affinity chromatography on mercaptoethylamine-Sepharose |
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Authors: | A. Plá A Chueca J López-Gorgé |
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Affiliation: | (1) Unidad de Bioquímica Vegetal, Estación Experimental del Zaidín (C.S.I.C.), Granada, Spain |
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Abstract: | A new purification procedure for spinach leaf fructose-1,6-bisphosphatase is proposed, which includes the use of affinity chromatography on mercaptoethylamine-Sepharose. A homogeneous preparation of the enzyme can be obtained in 48 hr, with a specific activity of 67 U/mg and a yield of 23%. The method may also be useful for the purification of other thioredoxin-activated chloroplast enzymes. |
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Keywords: | affinity chromatography enzyme purification fructose-1,6-bisphosphatase spinach |
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