A versatile assay for gelatinases using succinylated gelatin

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 metalloprotei...

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Bibliographic Details
Published in:Matrix biology 2000-07, Vol.19 (3), p.267-273
Main Authors: Baragi, Vijaykumar M., Shaw, Bonnie J., Renkiewicz, Richard R., Kuipers, Paul J., Welgus, Howard G., Mathrubutham, Mahesh, Cohen, Jon R., Rao, Srinivasa K.
Format: Article
Language:English
Subjects:
Gelatin - metabolism
Gelatinases - antagonists & inhibitors
Gelatinases - metabolism
Humans
Hydrolysis
Matrix Metalloproteinase 2 - metabolism
Matrix Metalloproteinase 9 - metabolism
Metalloendopeptidases - antagonists & inhibitors
MMP-2
MMP-9
Phenylalanine - analogs & derivatives
Phenylalanine - pharmacology
Spectrophotometry
Substrate Specificity
Succinates - metabolism
Succinic Acid - metabolism
Succinylated-gelatin
Thiophenes - pharmacology
Tumor Cells, Cultured
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Summary: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 (
ISSN:0945-053X
1569-1802
DOI:10.1016/S0945-053X(00)00086-X