Factor bovine

Sequences have been determined for plasminogen and bovine Factor XII, and they are not homologous with the other serine proteases. The amino-terminal sequence of Factor XII is homologous, however, with the active site of several naturally occurring protease inhibitors (11). 

Sturzebecher J, Sturzebecher U, Yieweg H, Wagner G, Hauptmann J, Markwardt F. Synthetic inhibitors of bovine factor Xa and thrombin comparison of their anticoagulant efficiency. Thrombosis Res 1989 54 245-252. 

Wei A, et al. Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J. Mol. Biol. 1998 283 147-154. 

Linked fucose has been found on the EGF domains of urokinase, tissue plasminogen activator (tPA), factor VII, and factor XII, attached to the consensus sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys. The fucosyltransferase responsible for the initiation of this type of gly-cosylation has been cloned [165]. On human (but not bovine) factor IX the tetrasaccharide Neu5Ac(o 2-6)Gal(jSl—4)GlcNAc( 81-3)Fuc(al-0)Ser (O Fig. 13d) was found [166,167]. In other FGF domains only Fuc(a l-0)Ser/Thr was detected. 

L12. Lindquist, P. A., Fujikawa, K., and Davie, E. W., Activation of bovine Factor IX (Christmas Factor) by Factor XI. (activated plasma thromboplastin antecedent) and a protease from Russell s viper venon. J. Biol. Chem. 253, 1902-1909 (1978). 

N2. Neisheim, M. E., and Mann, K. G., Thrombin catalyzed activation of single chain bovine Factor V. J. Biol. Chem. 254, 1326-1334 (1979). 

The effect of deglycosylation of bovine factor XI has been investigated with factor-X-activating enzyme from Russell s viper venom or extrinsic Xase (factor Vlla/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase [52]. The removal of 0-linked carbohydrate resulted in a decrease in the rate of activation. 

Eujikawa, K., Legaz, M.E., Kato, H., Davie, E.W. 1974. The mechanism of activation of bovine factor IX (Ghristmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent). Biochemistry 13, 4508-4516. 

Source Courtesy of Haematologic Technologies, Inc., Essex Junction, VT, Research Reagents Catalog, 2004-2005. Inferred from the zymogen, factor XL Based upon analysis of bovine factor VII. 

The amino acid sequences of human prothrombin (4,5), bovine prothrombin (3), bovine factor IX (93), bovine factor X (6,7), bovine protein C (94,95) and bovine protein S (96) have been determined. In addition, the amino acid sequences of bovine... 

Nakamura, S., Iwanaga, S., Suzuki, T., Mikuni, Y., Konishi, K. Amino acid sequence of the peptide released from bovine factor XIII following activation by thrombin. Biochem. biophys. Res. Commun. 58, 250-256... 

The role of Ca in bovine factor IX structure and activation has been examined. Although several cations effectively interact with factor IX, there appears to be a rigid specificity for the cation in the activation of this proenzyme by the intrinsic coagulation system. The lack of co-operative interactions in the binding... 

Habu IX/X-bp as anticoagulant protein has been isolated originally from the crude venom of T flavoviridis using an affinity chromatography column of insolubilized bovine factor X (7). We are now able to prepare this protein in a large scale by ion-exchange... 

Binding of IX/X-bp to factors IX and X is dependent on the concentration of calcium ions. Half-maximal binding to factors IX and X of IX/X-bp occurs at 0.39 mM and 0.35 mM calcium ions, respectively. Maximal binding is observed at 1 mM calcium ions. The binding affinity of IX/X-bp for factor IX is compared with that of IX/X-bp for factor X in the presence of 1 mM calcium ions (18). IX/X-bp binds to factor IX at lower concentrations than to factor X. The apparent Kd values for binding of IX/X-bp to solid-phase bovine factors IX and X are calculated to be 0.36 nM and 1.13 nM, respectively (Table I). IX/X-bp binds to the activated forms of factors IX and X (bovine factor IXa and bovine factor Xa) in a similar manner. The binding affinities of IX/X-bp for human factors IX and X are also essentially the same. IX/X-bp does not bind to solid-phase bovine factor VII or to other vitamin K-dependent Gla-containing proteins, such as bovine prothrombin, protein C, protein Z, and human protein C at the concentrations tested (up to 670 nM). 

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