title: Method of purification of thiol proteinase inhibitors from human urine.
abstract: Urinary thiol proteinase inhibitors (UTPI) had been isolated from their complex with papain. Almost 90% of these inhibitors, previously inactivated by native or immobilized papain, were recovered after heating the complex to 80 degrees C at pH 2.0 for 20 min. Two protein inhibitors with molecular weights of 76,000 (UTPI-76) and about 45,000 (UTPI-45) were isolated from urine of patients with malignant colorectal tumor. UTPI-fraction consisted of about 40% of UTPI-76 (probably light form of kininogen) and of 60% of UTPI-45 fraction. The inhibitors differed in affinity to Concanavalin A. No electrophoretic mobility changes of both UTPI, before and after isolation by described affinity chromatography were observed.
authors.affiliation: Department of Biochemistry, Medical School of Wrocław, Poland.
authors.forename: M
authors.initials: M
authors.lastname: Siewiński
mesh_terms: D002845:Chromatography; D015179:Colorectal Neoplasms / Q000652:urine; D015853:Cysteine Proteinase Inhibitors / Q000652:urine*; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008722:Methods; D008970:Molecular Weight; D010206:Papain
chemical_list: D015853:Cysteine Proteinase Inhibitors; D010206:Papain