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Characterization of two glycoprotein variants of bovine factor X and demonstration that the factor X zymogen contains two polypeptide chains

Biochemistry 11(26): 4873-4882

Characterization of two glycoprotein variants of bovine factor X and demonstration that the factor X zymogen contains two polypeptide chains

Accession: 015253515

PMID: 4638344

DOI: 10.1021/bi00776a001

Related references

Jackson C.M., 1972: Characterization of 2 glyco protein variants of bovine factor x and demonstration that the factor x zymogen contains 2 poly peptide chains. Biochemistry 11(26): 4873-4882

Chaudhuri, A.; Stringer, E.A.; Valenzuela, D.; Maitra, U., 1981: Characterization of eukaryotic initiation factor 2 containing two polypeptide chains of Mr = 48,000 and 38,000. Journal of Biological Chemistry 256(8): 3988-3994

Kerr, M.A.; Grahn, D.T.; Walsh, K.A.; Neurath, H., 1978: Activation of bovine factor X (Stuart factor)--analogy with pancreatic zymogen-enzyme systems. The activation of bovine coagulation factor X has been studied by kinetic and spectrophotometric measurements. The pH dependence of the hydrolysis of specific ester substrates by activated factor Xa can be ascribed to two independently ionizing gr...

Mizuochi, T.T.niguchi, T.F.jikawa, K.T.tani, K.K.bata, A., 1983: The structures of the carbohydrate moieties of bovine blood coagulation factor IX (Christmas factor)--occurrence of penta- and tetrasialyl triantennary sugar chains in the asparagine-linked sugar chains. Journal of biological chemistry, 258(10): 6020-6022

Walker, F.J., 1992: Characterization of the interaction between the heavy and light chains of bovine factor Va. Bovine factor Va has been previously been shown to consist of heavy (M(r) = 94,000) and light chains (M(r) = 81,000), that interact in a manner dependent upon the presence of either calcium or manganese ions. In an attempt to understand the mechan...

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Byatt, J.C.; Larson, B.R.; Baganoff, M.P.; McGrath, M.F.; Collier, R.J., 1990: Purification and partial characterization of a bovine epidermal growth factor-like polypeptide. A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to s...

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Castillo, M.; Kurachi, K.N.shino, N.O.kubo, I.P.wers, J., 1983: Reactivity of bovine blood coagulation factor IXalphabeta, factor Xalphabeta, and factor XIalpha toward fluorogenic peptides containing the activation site sequences of bovine factor IX and factor X. Biochemistry 22(5): 1021-1029