The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity

Recombinant tissue inhibitor of metalloproteinases (TIMP-1) and a truncated version containing only the three N-terminal loops, delta 127-184TIMP, have been expressed in myeloma cells and purified by affinity chromatography and gel filtration. delta 127-184TIMP was found to exist as two main glycosy...

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Veröffentlicht in:	Biochemistry (Easton) 1991-08, Vol.30 (33), p.8097-8102
Hauptverfasser:	Murphy, Gillian, Houbrechts, Annick, Cockett, Mark I, Williamson, Richard A, O'Shea, Mark, Docherty, Andrew J. P
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Biological and medical sciences Electrophoresis, Polyacrylamide Gel Enzyme Stability Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glycoproteins - chemistry Glycoproteins - genetics Glycoproteins - isolation & purification Humans Hydrolases Macromolecular Substances Metalloendopeptidases - antagonists & inhibitors metalloproteinase Mice Molecular Sequence Data Plasmacytoma Rabbits Recombinant Proteins - genetics Tissue Inhibitor of Metalloproteinases Tumor Cells, Cultured
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