Factor XI: purification from porcine plasma by affinity chromatography and some properties of factor XI and activated factor XI.
Porcine factor XI and activated factor XI were purified by the introduction of affinity chromatography on high molecular mass kininogen. On the affinity chromatography, it was observed that high affinity exists between porcine factor XI and high molecular mass kininogen. In the preparation, however, factor XII, plasma prekallikrein and high molecular mass kininogen were not detected. The factor XI forms a dimer, and is a heterogeneous molecule, judging from sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Substrate specificity of activated factor XI and inhibition profile of activated factor XI against proteinase inhibitors were investigated by comparison with those of bovine and human activated factor XI. From these results, the properties of porcine activated factor XI show great similarities with those of bovine and human activated factor XI.
Mashiko
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H
Division of Chemistry of Hygiene, Meiji College of Pharmacy, Tokyo, Japan.
Takahashi
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H
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005172:Factor XI / Q000302:isolation & purification* / Q000378:metabolism; D005174:Factor XII / Q000378:metabolism; D015945:Factor XIa / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D013552:Swine
D005174:Factor XII; D005172:Factor XI; D015945:Factor XIa