title: Purification of factor XI and some properties of activated factor XI from porcine plasma.
abstract: Porcine Factor (F.) XI was purified by following three successive chromatographies. By this procedure, about 5.5 mg of F. XI was obtained from 500 ml of the plasma. The F. XI forms dimer, and is heterogeneous molecule, judging from SDS-polyacrylamide gel electrophoresis. The properties of isolated porcine F. XIa are great similar with those of bovine F. XIa.
authors.affiliation: Meiji College of Pharmacy, Tokyo, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Mashiko
authors.forename: H
authors.initials: H
authors.lastname: Takahashi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005172:Factor XI / Q000302:isolation & purification* / Q000378:metabolism*; D015945:Factor XIa / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine
chemical_list: D009842:Oligopeptides; D005172:Factor XI; D015945:Factor XIa