A Fluorometric Method for Dipeptidase Activity Measurement in Urine, Using L-Alanyl-L-Alanine as Substrate
| Autor: | Kazuyuki Hirano, Mamoru Sugiura, Shunji Sawaki, Yoshimasa Ito, Taro Ogiso, Yoshihito Watanabe |
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| Rok vydání: | 1984 |
| Předmět: |
Dipeptidase
Dipeptidases Immunodiffusion medicine.medical_specialty Urinary system medicine.medical_treatment Fluorescence spectrometry Urine Kidney Biochemistry Substrate Specificity chemistry.chemical_compound Internal medicine medicine Humans Molecular Biology Dialysis Dihydrolipoamide Dehydrogenase Creatinine biology Dipeptides General Medicine Electrophoresis Disc medicine.disease Spectrometry Fluorescence medicine.anatomical_structure Endocrinology Alanine Dehydrogenase chemistry biology.protein Kidney Diseases Amino Acid Oxidoreductases Nephrotic syndrome |
| Zdroj: | The Journal of Biochemistry. 96:1-8 |
| ISSN: | 1756-2651 0021-924X |
| DOI: | 10.1093/oxfordjournals.jbchem.a134801 |
| Popis: | A new method for the measurement of urinary dipeptidase activity is described. The action of dipeptidase on L-Ala-L-Ala results in production of an L-alanine, and this amino acid is simultaneously determined by an L-alanine dehydrogenase-diaphorase system. As urinary substances do not affect this reaction, the measurement can be accomplished without prior dialysis. The mean value +/- S.D. for normals was found to be 12.0 +/- 4.4 IU/g of creatinine. Elevated values were found in chronic nephritis (55.9 +/- 35.0 IU/g of creatinine, P less than 0.001 vs. normal), acute nephritis (46.6 +/- 29.9 IU/g of creatinine, P less than 0.001), and nephrotic syndrome (43.3 +/- 36.5 IU/g of creatinine, P less than 0.001). The dipeptidase activity thus measured showed a significant correlation with dipeptidase activity against L-Leu-L-Leu as substrate. On disc polyacrylamide gel electrophoresis, the urinary dipeptidase of a patient with chronic nephritis appeared as one band with similar mobility to human kidney dipeptidase F. Urinary dipeptidase in a patient with chronic nephritis was identical to human kidney dipeptidase on double immunodiffusion analysis. |
| Databáze: | OpenAIRE |
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