User:Francis Ayombil

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Graduate student at the University of Vermont,VT. Folks check out my page on the coagulation enzyme known as '''Factor XIa'''. [http://proteopedia.org/wiki/index.php/Factor_XIa. This particular serine protease is unique in that compared to other cylindrical
Graduate student at the University of Vermont,VT. Folks check out my page on the coagulation enzyme known as '''Factor XIa'''. [http://proteopedia.org/wiki/index.php/Factor_XIa. This particular serine protease is unique in that compared to other cylindrical
vitamin K-dependent coagulation proteases, this enzyme is a dimer whose monomer subunits are connected by a disulfide bond. This enzyme belongs to the chymotrypsin-like serine protease family. Factor XIa is found in the contact pathway of the hemostatic response following an injury where it activates Factor IX to Factor IXa in the classical waterfall model of the blood coagulation.
vitamin K-dependent coagulation proteases, this enzyme is a dimer whose monomer subunits are connected by a disulfide bond. This enzyme belongs to the chymotrypsin-like serine protease family. Factor XIa is found in the contact pathway of the hemostatic response following an injury where it activates Factor IX to Factor IXa in the classical waterfall model of the blood coagulation.

Current revision


Graduate student at the University of Vermont,VT. Folks check out my page on the coagulation enzyme known as Factor XIa. [http://proteopedia.org/wiki/index.php/Factor_XIa. This particular serine protease is unique in that compared to other cylindrical vitamin K-dependent coagulation proteases, this enzyme is a dimer whose monomer subunits are connected by a disulfide bond. This enzyme belongs to the chymotrypsin-like serine protease family. Factor XIa is found in the contact pathway of the hemostatic response following an injury where it activates Factor IX to Factor IXa in the classical waterfall model of the blood coagulation.

Proteopedia Page Contributors and Editors (what is this?)

Francis Ayombil, Eran Hodis

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