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[Aspartate kinase activity of Cyanobacteria Anabaena variabilis].

作者信息

Lysenko T G, Koltukova N V, Kadyrova G Kh, Shainskaia O A

出版信息

Ukr Biokhim Zh (1978). 1993 Nov-Dec;65(6):61-6.

PMID:8048183
Abstract

Aspartate-kinase (ASK) activity of filamentous cyanobacteria A. variabilis and its dependence on physico-chemical factors and substrate concentration in the reaction mixture have been studied. Three isoenzymes ASK-1, ASK-2 and ASK-3 which differ in the values of pH-optima, molecular weight, isoelectric points and effector of retro-inhibition have been isolated by ion-exchange chromatography. High level of inhibition of summary ASK of the cell-free extract can be reached only in a case of simultaneous addition of all amino acids, the final products of this biosynthetic pathway into the incubation mixture.

摘要

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