title: [Affinity chromatography of human gamma-thrombin on fibrin-agarose].
abstract: gamma-Thrombin was produced during autolysis or limited proteolysis of coagulant gamma-thrombin. This thrombin form loses its ability to coagulate fibrinogen but preserves the esterase and amidase activity on the low-molecular-weight synthetic substrates. This evidences for the integrity of the active site of gamma-thrombin and for the integrity break of the enzyme molecule region responsible for the binding with fibrinogen. gamma-Thrombin with the minimal coagulating activity, possessing high esterase and amidase activity is obtained. Fibrin-agarose possessing affinity to gamma-thrombin and specifically not binding gamma-thrombin was used to remove admixtures of the coagulant gamma-thrombin from the preparations of gamma-thrombin obtained during the enzyme autolysis.
authors.forename: L P
authors.initials: LP
authors.lastname: Shvachko
authors.forename: V K
authors.initials: VK
authors.lastname: Kibirev
mesh_terms: D002384:Catalysis; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005337:Fibrin; D006801:Humans; D012685:Sepharose; D013917:Thrombin / Q000032:analysis*
chemical_list: D005337:Fibrin; D012685:Sepharose; D013917:Thrombin
vernacular_title: Afinnaia khromatografiia gamma-trombina cheloveka na fibrin-agaroze.