Add time:08/20/2019         Source:sciencedirect.com

Publisher SummaryCysteinesulfinic acid (CSA), or β-sulfinyl-α-aminopropionic acid, is accepted as a structural analog of aspartic acid by the L-aspartate amino-transferase (glutamic-oxaloacetic transaminase) from both animal and bacterial sources. Evidence for that conclusion is found in the competitive relationship between CSA and aspartate as alternative substrates for the enzyme. When augmented with a colorimetric determina tion of the sulfite released, the reaction of CSA with α-ketoglutarate in the presence of aspartate aminotransferase provides a convenient, reliable, and precise method for the determination of CSA. To demonstrate the adequacy of the method, appropriate amounts of a neutral solution of CSA are combined with 15 μmol α-ketoglutarate and 210 μmol of the phosphate buffer in a total volume of 2.4 ml. The reaction is initiated by the addition of 25 units of enzyme in a volume of 100 μl. A control for inorganic sulfite indigenous to the samples is performed by adding the KOH and HgCl2 prior to addition of the aminotransferase. Such controls are not incubated at 37° but are centrifuged directly and combined with fuchsin reagent.

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