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Clinical Chemistry 19: 756-761, 1973;
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Clinical Chemistry, Vol 19, 756-761, Copyright © 1973 by the American Association for Clinical Chemistry

Evaluation of S-Benzyl-L-cysteine-4'-nitroanilide as a Substrate for Serum Cystine Aminopeptidase

J. E. Tovey 1, P. J. G. Dawson 1, and K. P. Fellowes 1

1 Department of Pathology, Worthing Hospital, Worthing, Sussex, England (J. E. T.); and the Clinical Reagent Development Department, BDH Chemicals Ltd., Poole, Dorset, England (P. J. G. D. and K. P. F.).

Under appropriate conditions, S-benzyl-L-cysteine-4'-nitroanilide is rapidly hydrolyzed by serum cystine aminopeptidase. The enzyme may be estimated kinetically by determining the rate of liberation of 4-nitroaniline. A simple automated procedure has been devised, and 50 samples of pregnancy sera can be analyzed per hour by use of the LKB 8600 Reaction Rate Analyzer. The correlation coefficient between results of this method and those obtained with L-cystine-di-4'-nitroanilide as substrate was 0.97.


Key Words: automated procedure with use of LKB Analyzer • detecting abnormal pregnancies • management of pregnancy • oxytocin degradation

Submitted on March 13, 1973
Accepted on May 7, 1973






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Copyright © 1973 by the American Association for Clinical Chemistry.