A versatile assay for gelatinases using succinylated gelatin
| Autor: | Vijaykumar M. Baragi, Mahesh Mathrubutham, Howard G. Welgus, Paul J. Kuipers, Bonnie J. Shaw, Jon R. Cohen, Richard R. Renkiewicz, Srinivasa K. Rao |
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| Rok vydání: | 2000 |
| Předmět: |
Gelatinases
Phenylalanine Gelatin Zymography Succinic Acid Peptide Thiophenes Matrix metalloproteinase Substrate Specificity Hydrolysis Tumor Cells Cultured Humans Molecular Biology chemistry.chemical_classification Metalloendopeptidases Substrate (chemistry) Succinates Enzyme Matrix Metalloproteinase 9 Biochemistry chemistry Spectrophotometry Gelatin Matrix Metalloproteinase 2 Succinylated gelatin |
| Zdroj: | Matrix Biology. 19:267-273 |
| ISSN: | 0945-053X |
| DOI: | 10.1016/s0945-053x(00)00086-x |
| Popis: | A spectrophotometric assay using succinylated gelatin as substrate is described for measuring the catalytic activity of gelatinases. The assay is based on measurement of primary amines exposed as a result of hydrolysis of the substrate by gelatinases. Comparison of hydrolysis by matrix metalloproteinase (MMP) 1, 2, 3, 7, 9 indicated that succinylated gelatin was primarily digested by MMP-2 and -9. The assay is rapid ( |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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