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- W1452451700 abstract "Publisher Summary This chapter presents the procedure for purification and assaying of mammalian collagenases, which proteinases acting at neutral pH to cleave the native helix of the interstitial collagens. Collagenase can be purified from the culture media of a variety of tissues or cells from different species. The purification steps include: ammonium sulfate precipitation; gel filtration with ultrogel AcA 44; DEAE-cellulose chromatography; and zinc chelate affinity chromatography. At the present time, only assay systems employing collagen itself as a substrate are suitable for the unambiguous detection of specific collagenases. Type I collagen is normally used as the substrate for the assay of collagenase and is prepared in soluble form from skin and tendon. Soluble collagen can be reconstituted into insoluble fibrils by incubating at 25-37°C at neutral pH and this provides the basis for the most widely used collagenase assays. Radiolabeled collagen fibrils are incubated with the enzyme and collagen degradation followed by the assay of radioactivity solubilized during the assay period." @default.
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- W1452451700 date "1981-01-01" @default.
- W1452451700 modified "2023-09-25" @default.
- W1452451700 title "[52] Mammalian collagenases" @default.
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- W1452451700 doi "https://doi.org/10.1016/s0076-6879(81)80054-7" @default.
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