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

Autor: Braman JC, Black MJ, Mangum JH
Jazyk: angličtina
Zdroj: Preparative biochemistry [Prep Biochem] 1981; Vol. 11 (1), pp. 23-32.
DOI: 10.1080/00327488108068723
Abstrakt: 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.
Databáze: MEDLINE