Homogeneous enzymatic assay for L-cysteine with betaC-S lyase.

Bioscience, biotechnology, and biochemistry (2005-11-25)
Yoshiaki Nishiya, Yasuo Yoshida, Mamiko Yoshimura, Haruka Fukamachi, Yoshio Nakano
RESUMEN

We have developed a new enzymatic assay for determining L-cysteine concentration. The method involves the use of betaC-S lyase from Streptococcus anginosus, which catalyzes the alpha,beta-elimination of L-cysteine to hydrogen sulfide, pyruvate, and ammonia. The production of pyruvate is measured by D-lactate dehydrogenase and NADH. The decrease in NADH was proportional to the L-cysteine concentration up to 1.0 mM. When serum samples were used, within-day and day-to-day coefficient variations were below 4%. This method is simple, and can easily and reliably be used for accurate determination of L-cysteine concentration in serum or other samples.

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