title: Functional Kunitz inhibitor binding domain in plasmin-derived light chain as shown by affinity chromatography.
abstract: The light chain of plasmin, prepared by selective reduction of the interchain disulfide bridges, can be separated from the heavy chain by affinity adsorption onto Kunitz inhibitor/Sepharose. This adsorption involves the active center of plasmin because it does not occur if the light chain is derived from a plasmin previously blocked by the active site titrant p-nitrophenyl-p'-guanidinobenzoate. It can be deduced that the conformation of the inhibitor binding domain of plasmin is preserved in the free light chain.
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002846:Chromatography, Affinity / Q000379:methods; D005260:Female; D005341:Fibrinolysin / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000302:isolation & purification* / Q000378:metabolism; D010920:Placenta / Q000201:enzymology; D010958:Plasminogen / Q000302:isolation & purification; D011247:Pregnancy; D011485:Protein Binding; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000378:metabolism
chemical_list: D046911:Macromolecular Substances; D010446:Peptide Fragments; D010958:Plasminogen; D014360:Trypsin Inhibitor, Kunitz Soybean; D005341:Fibrinolysin