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Using the method of affinity chromatography on NAD-Sepharose, themyo-inositol-1-phosphate synthase (EC 5.5.1.4) from testicles of the bull could be purified to homogeneity. Although its specificity, its activity and its molecular weight are all very similar to the corresponding properties of the enzyme from rat testicles, there are also some considerable differences between the two enzyme proteins. Whereas the rat enzyme consists of two different pairs of subunits with the molecular weights of 3.5×104 and 7.2×104, respectively, the bull enzyme consists of four subunits, all of them apparently having the same molecular weight of 5.45×104. The isoelectric points of the two enzyme proteins are also different; with the help of the method of isoelectric focussing they were determined as 3.95 for the rat enzyme and 4.59 for the enzyme from the bull.  相似文献   

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Ohne Zusammenfassung Die hier berichteten Versuche wurden in den Jahren 1932–33 ausgeführt. Ein kurzer Bericht findet sich in einer Zusammenfassung (1) der Institutsarbeiten über das kolloide Gold.  相似文献   

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A Rapid Purification of D -Oxynitrilase from Almond Meal by Affinity Chromatography Oxynitrilase from almond meal is capable of catalyzing the stereospecific addition of cyanide to a variety of aldehydes. Thus, the enzyme is potentially useful in the synthesis of optically active cyanohydrins on a preparative scale [1]. As the currently available purification procedures for this enzyme [2] are rather tedious, we have elaborated a simple and rapid procedure based on affinity chromatography. An inhibitor for the enzyme, methyl p-(3-aminopropoxy)benzoate (4) , has been synthesized and attached covalently to Sepharose 4B as a solid matrix (5) . With this affinity gel it was possible to prepare the D -oxynitrilase in a simple procedure with high yields.  相似文献   

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