title: Partial purification and characterization of the enzyme which converts precursor liver protein to factor X.
abstract: A rat liver post-microsomal supernatant enzyme, which carries out an epigenetic conversion of a protein contained in liver microsomes to Factor X, has been partially purified 250-fold in 50% yield by a combination of salt fractionation and gel filtration. The crude enzyme is stable to freezing and thawing but unstable at 4 degrees C. However, the partially purified enzyme is more stable at 4 degrees C. It requires Ca2+ and HCO3 minus for optimum formation of Factor X activity. The supernatant enzyme is vitamin K dependent and exhibits its maximum rate of formation of Factor X between pH 8 and 8.5.
mesh_terms: D000818:Animals; D001639:Bicarbonates / Q000494:pharmacology; D001777:Blood Coagulation; D001779:Blood Coagulation Factors / Q000378:metabolism; D002118:Calcium / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D004798:Enzymes / Q000302:isolation & purification / Q000378:metabolism*; D005170:Factor X / Q000096:biosynthesis*; D006863:Hydrogen-Ion Concentration; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D051381:Rats; D014812:Vitamin K / Q000494:pharmacology; D014859:Warfarin / Q000494:pharmacology
chemical_list: D001639:Bicarbonates; D001779:Blood Coagulation Factors; D004798:Enzymes; D014812:Vitamin K; D010664:Phenylmethylsulfonyl Fluoride; D014859:Warfarin; D005170:Factor X; D002118:Calcium