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Enzymes and Protein Markers |
1
Max-Planck Research Unit, Enzymology of Protein Folding, Kurt-Mothes Str. 3, D-06120 Halle/Saale, Germany.
2
Martin-Luther-University Halle-Wittenberg, Institut for
Clinical Chemistry and Pathobiochemistry, Madgeburger Str., D-06112
Halle/Saale, Germany.
a Author for correspondence. Fax +49345 5511972;
An UV/VIS spectrophotometric assay technique was developed that was able to routinely monitor peptidylprolyl cis/trans isomerase (PPIase) activity of biological fluids in 96-well microtiter plates. The assay, based on monitoring the cis-to-trans isomerization of succinyl-Phe-cisPro-Phe-4-nitroanilide as substrate in a chymotrypsin-coupled reaction, yields a throughput of 96 samples per 30 min. The assay's capacity was exemplified by dealing with the PPIase activity in several normal and pathological human sera. Reference values of 151 healthy subjects (83 females, 69 males, 17 to 60 years old) were found to possess significant sex-specific differences. PPIase activity factor K of the sera was significantly greater in males (5th, 50th, 95th percentiles: 17, 36, 55 K) than females (14, 30, 48 K). PPIase activities of sera from healthy donors (n = 151) were significantly higher (MannWhitney rank-sum test P <0.0001) than those of patients (n = 47). PPIase activity in serum samples stored at 4 °C was stable for at least 20 h.
The following articles in journals at HighWire Press have cited this article:
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