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Bovine Factor V was incubated briefly with bovine β- thrombin, causing partial conversion to Factor Va. QAE- cellulose chromatography in Ca++ of the partially activated material yielded 3 fractions. Electrophoresis in DodSO4 indicated primarily starting material (Mr=330,000) in the first fraction; two peptides of Mr=150,000 and 200,000 in the second; and two peptides of Mr=200,000 and 90,000 in the third. The first of these latter fractions was active only after further incubation with thrombin, while the other was active without further thrombin catalyzed activation. After thrombin treatment both fractions had specific activities equal to that of fully activated, unfractionated Factor V. Incubation of either of these fractions with EDTA caused complete loss of activity and allowed isolation of the constituent polypeptides by further chromatography on QAE- cellulose in EDTA. The NH2-termini of the 150,000 and 90.000 apparent Mr peptides had sequences identical to that of Factor V. The 200,000 apparent Mr peptides of the two fractions obtained by chromatography in Ca++ had NH2- terminal sequences identical to each other but different from that of Factor V. The summed amino acid compositions of the Mr=200,000 and Mr=150,000 were equivalent to that of Factor V. Electrophoretic analysis indicated that thrombin converts the Mr=150,000 peptide to endproducts of Mr=90,000 and 71,000, and the Mr=200,000 peptide to endproducts of 83.000 and 31,000 apparent Mr. Recalcification of the individual isolated intermediates, followed by incubation with thrombin did not yield cofactor activity. Recombina- ion of the recalcified intermediates followed by incubation with thrombin, however, generated samples with activities approaching that of unfractionated, activated Factor V. These data indicate that the intermediates of Mr=150,000 and Mr=200,000 arise by a single cleavage of Factor V, and that Factor Va comprises peptides derived from both of these intermediates.

Isolation And Properties Of Intermediates Involved In Thrombin-Catalyzed Conversion Of Bovine Factor V To Factor Va