Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme

We have recently cloned MMP-19, a novel matrix metalloproteinase, which, due to unique structural features, was proposed to represent the first member of a new MMP subfamily (Pendás, A. M., Knäuper, V. , Puente, X. S., Llano, E., Mattei, M. G., Apte, S., Murphy, G., and López-Otin, C. (1997) J. Biol...

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Veröffentlicht in:	The Journal of biological chemistry 2000-05, Vol.275 (20), p.14809-14816
Hauptverfasser:	Stracke, J O, Hutton, M, Stewart, M, Pendás, A M, Smith, B, López-Otin, C, Murphy, G, Knäuper, V
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Basement Membrane - metabolism Catalytic Domain Cloning, Molecular Escherichia coli gelatin Humans Matrix Metalloproteinases, Secreted Metalloendopeptidases - chemistry Metalloendopeptidases - metabolism MMP-19 protein Molecular Sequence Data Mutagenesis nidogen Oligopeptides - chemistry Oligopeptides - metabolism Peptide Fragments - chemistry Peptide Fragments - metabolism Polymerase Chain Reaction Protein Denaturation Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sequence Deletion Substrate Specificity
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