title: Localization of the structural difference between bovine blood coagulation factors X1 and X2 to tyrosine 18 in the activation peptide.
abstract: Bovine Factor X is isolated in two chromatographically separable forms, Factor X1 and Factor X2. Whereas only a single form of Factor Xa, the active protease, exists, the activation peptides also exist as two chromatographically distinct species. These peptides have been shown to differ at a tyrosyl residue by ultraviolet spectrophotometry, and in their composition after alkaline hydrolysis. On the basis of the spectral properties, and elution position of the modified tyrosine on Dowex 1 columns and on an amino acid analyzer, it has been concluded that Factor X2 contains a tyrosyl-O-SO4 residue at position 18 in the activation peptide whereas Factor X1 contains only tyrosine. Alternative explanations such as differences in carbohydrate composition, differences in phosphate content, or differences in the number of gamma-carboxyglutamic acid residues were demonstrated to be unrelated to the difference in chromatographic behavior between bovine Factors X1 and X2.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D005170:Factor X / Q000032:analysis*; D015951:Factor Xa; D010446:Peptide Fragments / Q000032:analysis; D012794:Sialic Acids / Q000032:analysis; D014443:Tyrosine / Q000032:analysis*
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D012794:Sialic Acids; D014443:Tyrosine; D005170:Factor X; D015951:Factor Xa