Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities
| Autor: | Christopher W. Sutton, Sarojani Angal, Gillian Murphy, P A Koklitis |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Matrix Metalloproteinase 3
Hot Temperature Molecular Sequence Data Gingiva Biochemistry Chromatography Affinity law.invention Type IV collagen law Casein Humans Amino Acid Sequence Molecular Biology Polyacrylamide gel electrophoresis Cells Cultured Glycoproteins chemistry.chemical_classification Enzyme Precursors biology Chemistry Metalloendopeptidases Tissue Inhibitor of Metalloproteinases Cell Biology Fibroblasts Peptide Fragments Recombinant Proteins Enzyme Activation Molecular Weight Kinetics Enzyme Proteoglycan biology.protein Recombinant DNA Electrophoresis Polyacrylamide Gel Elastin Research Article |
| Zdroj: | Biochemical Journal. 276:217-221 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2760217 |
| Popis: | Recombinant human prostromelysin was purified in a single step using Procion Red-Sepharose chromatography. The purified prostromelysin was self-activated to high-Mr (45,000) and low-Mr (28,000) forms by incubation at 55 degrees C without the addition of extraneous activators. The two forms of stromelysin were subsequently separated, again using Procion Red-Sepharose. Both of the heat-activated recombinant forms demonstrated similar specific activities (for the macromolecular substrates casein, gelatin, elastin, proteoglycan and type IV collagen) when compared with either heat- or trypsin-activated natural stromelysin. The heat-activated recombinant stromelysins both showed similar abilities to potentiate activation of human procollagenase when compared with trypsin-activated natural stromelysin. |
| Databáze: | OpenAIRE |
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