FEBS Letters · 1985 · 41 citations · 21 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProtein-protein InteractionsEnzyme FunctionEnzyme InhibitionPlasma ProteinsProtein BindingProtein StructureProteolytic EnzymesProtease Cleavage SpecificityProtease InhibitionProtease Inhibition MechanismsProtease Inhibitor InteractionsProtease InhibitorsProtein Structural ChangesProteolytic Enzyme Activity
The overall mechanism of interaction with proteinases of alpha 1-inhibitor3, a plasma proteinase inhibitor so far specific to the rat, has been shown to be closely similar to that described for alpha-macroglobulins. This mechanism includes: (i) the cleavage of at least one susceptible peptidic bond which leads to structural changes in the molecule. (ii) The cleavage of a putative thiol ester bond in another site of the molecule which permits the covalent linkage of the enzyme. Moreover, fragmentation of alpha 1-inhibitor3 upon heating as observed for alpha-macroglobulin quarter subunits has been demonstrated. The question is raised of the presence of such a molecule in rat plasma in addition to two alpha-macroglobulin species, all of these proteinase inhibitors being antigenically unrelated.
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Proteinases in mammalian cells and tissues
Michael Kerr · Biochemical Education · 1978 · 922 citations
Human α2-macroglobulin: structure and function
F VANLEUVEN · Trends in Biochemical Sciences · 1982 · 131 citations