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 introdu ction of affinity chromatography on high molecular mass kininogen. On the affinity chromatography, it was observed that high affinity exsist s between porcine factor XI and high molecular mass kininogen. In the preparation, however, factor XII, plasma prekallikrein and high molecu lar mass kininogen were not detected. The factor XI forms a dimer, and is a heterogeneous molecule, judging from sodium dodecyl sulfate-poly acrylamide gel electrophoresis. Substrate specificity of activated fac tor XI and inhibition profile of activated factor XI against proteinas e inhibitors were investigated by comparison with those of bovine and human activated factor XI. From these results, the properties of porci ne activated factor XI show great similarities with those of bovine an d human activated factor XI.