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dc.contributor.authorBunning, R
dc.contributor.authorMurphy, G
dc.contributor.authorKumar, Shant
dc.contributor.authorPhillips, P
dc.contributor.authorReynolds, J
dc.date.accessioned2011-03-08T16:24:02Z
dc.date.available2011-03-08T16:24:02Z
dc.date.issued1984-02-15
dc.identifier.citationMetalloproteinase inhibitors from bovine cartilage and body fluids. 1984, 139 (1):75-80 Eur J Biochemen
dc.identifier.issn0014-2956
dc.identifier.pmid6321174
dc.identifier.doi10.1111/j.1432-1033.1984.tb07978.x
dc.identifier.urihttp://hdl.handle.net/10541/123967
dc.description.abstractInhibitors of the mammalian metalloproteinases, collagenase, proteoglycanase and gelatinase were isolated from bovine cartilage (extracts and culture medium) and bovine amniotic fluid and serum. These inhibitors either bind or do not bind to concanavalin-A--Sepharose, with Mr (gel filtration) of about 30 000 and 20 000, respectively. Cartilage and chondrocyte culture media contained only concanavalin-A-binding inhibitors whereas cartilage extracts contained only a non-binding inhibitor: serum and amniotic fluid contained both forms of inhibitory activities. In moist biochemical respects, particularly in their abilities to inhibit metalloproteinases, all of the inhibitors were found to be similar. It is concluded that the forms of the inhibitors that differ in Mr may be closely related to the tissue inhibitor of metalloproteinases (TIMP) previously purified from rabbit and human sources. These findings help to clarify other studies on collagenase inhibitors and support the concept that TIMP-like inhibitors may be important in the control of connective tissue degradation.
dc.language.isoenen
dc.subject.meshAmniotic Fluid
dc.subject.meshAnimals
dc.subject.meshBlood
dc.subject.meshBody Fluids
dc.subject.meshCartilage
dc.subject.meshCattle
dc.subject.meshCulture Media
dc.subject.meshCulture Techniques
dc.subject.meshGelatinases
dc.subject.meshMetalloendopeptidases
dc.subject.meshMicrobial Collagenase
dc.subject.meshPepsin A
dc.subject.meshProtease Inhibitors
dc.subject.meshTissue Extracts
dc.subject.meshVitreous Body
dc.titleMetalloproteinase inhibitors from bovine cartilage and body fluids.en
dc.typeArticleen
dc.contributor.departmentCell Physiology Department, Strangeways Research Laboratory, Cambridgeen
dc.identifier.journalEuropean Journal of Biochemistryen
html.description.abstractInhibitors of the mammalian metalloproteinases, collagenase, proteoglycanase and gelatinase were isolated from bovine cartilage (extracts and culture medium) and bovine amniotic fluid and serum. These inhibitors either bind or do not bind to concanavalin-A--Sepharose, with Mr (gel filtration) of about 30 000 and 20 000, respectively. Cartilage and chondrocyte culture media contained only concanavalin-A-binding inhibitors whereas cartilage extracts contained only a non-binding inhibitor: serum and amniotic fluid contained both forms of inhibitory activities. In moist biochemical respects, particularly in their abilities to inhibit metalloproteinases, all of the inhibitors were found to be similar. It is concluded that the forms of the inhibitors that differ in Mr may be closely related to the tissue inhibitor of metalloproteinases (TIMP) previously purified from rabbit and human sources. These findings help to clarify other studies on collagenase inhibitors and support the concept that TIMP-like inhibitors may be important in the control of connective tissue degradation.


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