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Serine transhydroxymethylase: a simplified radioactive assay; purification and stabilization of enzyme activity employing Affi-Gel Blue.

作者信息

Braman J C, Black M J, Mangum J H

出版信息

Prep Biochem. 1981;11(1):23-32. doi: 10.1080/00327488108068723.

Abstract

An improved radioactive assay has been developed for serine transhydroxymethylase. This assay involves the direct measurement of the [14C]HCHO which is generated when [3- 14C]-serine is employed as the substrate. The new assay eliminates the need for a solvent extraction of a [14C]HCHO-dimedon adduct which is the basis of the assay devised by Taylor and Weissbach. The enzyme has been purified employing Affi-Gel Blue. The purified enzyme retains full activity when bound to this affinity chromatography matrix and can be stored in this state at 4 degrees indefinitely.

摘要

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