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 |
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| container_issue | 33 |
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| container_title | Biochemistry (Easton) |
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| creator | Murphy, Gillian Houbrechts, Annick Cockett, Mark I Williamson, Richard A O'Shea, Mark Docherty, Andrew J. P |
| description | 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 glycosylation variants of molecular mass 24 kD and 19.5 kDa and an unglycosylated form of 13 kDa. All forms of the truncated inhibitor were able to inhibit and form complexes with active forms of the matrix metalloproteinases, indicating that the major structural features for specific interaction with these enzymes resides in these three loops. Stable binding of delta 127-184TIMP to pro 95-kDa gelatinase was not demonstrable under the conditions for binding of full-length TIMP-1. |
| doi_str_mv | 10.1021/bi00247a001 |
| format | Article |
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Stable binding of delta 127-184TIMP to pro 95-kDa gelatinase was not demonstrable under the conditions for binding of full-length TIMP-1.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00247a001</identifier><identifier>PMID: 1868085</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>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. 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P</creatorcontrib><title>The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>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 glycosylation variants of molecular mass 24 kD and 19.5 kDa and an unglycosylated form of 13 kDa. All forms of the truncated inhibitor were able to inhibit and form complexes with active forms of the matrix metalloproteinases, indicating that the major structural features for specific interaction with these enzymes resides in these three loops. Stable binding of delta 127-184TIMP to pro 95-kDa gelatinase was not demonstrable under the conditions for binding of full-length TIMP-1.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Stability</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. 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| ispartof | Biochemistry (Easton), 1991-08, Vol.30 (33), p.8097-8102 |
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| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | 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 |
| title | The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity |
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