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• W2000475144 abstract "Recombinant plasminogen‐activator‐inhibitor type 1 (PAI‐1) purified in an active form from Escherichia coli and eucaryotic cells was found to contain a mixture of three functionally distinct forms: an active form that forms complexes with plasminogen activators (PAs), an inactive (latent) form that remains intact after incubation with PAs, and a substrate‐like form which is easily cleaved by PAs. Since active PAI‐1 purified from bacteria (rpPAI‐1) contains only trace amounts of the inactive latent and the substrate‐like forms, this material was used to study the effect of sodium dodecyl sulphate (SDS) on the structure and function of active PAI‐1. After treatment with 0.01% SDS, active rpPAI‐1 was converted to an inactive form that did not form complexes with PAs, but exhibited characteristics similar to those of latent PAI‐1. After treatment with 0.1% SDS, PAI‐1 lost its inhibitory activity and was cleaved as a substrate in the reactive center. Circular dichroism spectral analysis reveals that SDS changed the conformation of PAI‐1 dramatically, mainly by increasing its α‐helical content." @default.
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• W2000475144 date "1992-11-01" @default.
• W2000475144 modified "2023-10-17" @default.
• W2000475144 title "A substrate‐like form of plasminogen‐activator‐inhibitor type 1" @default.
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• W2000475144 doi "https://doi.org/10.1111/j.1432-1033.1992.tb17372.x" @default.
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