A new assay for L-asparagine synthetase

Journal of Biochemical and Biophysical Methods
C A Luehr, S M Schuster

Abstract

A fast, relatively inexpensive method of measuring the enzymatic formation of L-asparagine from L-aspartate is presented. This radiochemical assay requires simple manipulations making it ideal for working with large numbers of samples, while maintaining high sensitivity and reproducibility. A mechanism similar to the enzymatic beta-decarboxylation of aspartate is utilized but in a nonenzymatic reaction. In the presence of pyridoxal and A13+ ions, the 14C of L-[4-14C]aspartate is decarboxylated while L-[4-14C]asparagine remains intact. This assay is shown to be suitable for measuring mammalian L-asparagine synthetase activity, while not requiring the isolation of assay enzymes.

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Citations

Jan 1, 1981·The International Journal of Biochemistry·R K Beran, S M Schuster
Jan 1, 1984·Analytical Biochemistry·S UnnithanS M Schuster
Jan 1, 1991·Archives of Biochemistry and Biophysics·P M Mehlhaff, S M Schuster
Dec 8, 1981·Biochemistry·R S MarkinS M Schuster
Apr 1, 1989·European Journal of Clinical Microbiology & Infectious Diseases : Official Publication of the European Society of Clinical Microbiology·G R Benge
Mar 22, 1982·Life Sciences·D M Maul, S M Schuster
Oct 1, 1983·Journal of Bacteriology·K G MacPheeS M Schuster
Mar 1, 1985·Archives of Biochemistry and Biophysics·C A Luehr, S M Schuster
Nov 15, 1992·Archives of Biochemistry and Biophysics·M C Larsen, S M Schuster

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