Coagulation factor V exists uncomplexed in bovine plasma

Bovine coagulation factor V has been examined immunochemically to ascertain whether the coagulant polypeptide (h) with M r = 290 000–330 000 is complexed in plasma with a second immunochemically distinct polypeptide (I 2) of M r = 400 000. Antiserum containing antibodies to h and l 2 detects the l 2...

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Bibliographic Details
Published inBiochimica et biophysica acta. General subjects Vol. 714; no. 3; pp. 524 - 529
Main Authors Roy Ittyerah, T., Rawala, Razia, Colman, Robert W.
Format Journal Article
LanguageEnglish
Published Elsevier B.V 25.02.1982
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Summary:Bovine coagulation factor V has been examined immunochemically to ascertain whether the coagulant polypeptide (h) with M r = 290 000–330 000 is complexed in plasma with a second immunochemically distinct polypeptide (I 2) of M r = 400 000. Antiserum containing antibodies to h and l 2 detects the l 2 polypeptide eluting earlier than the h chain on gel filtration of plasma with either added calcium or EDTA, consistent with the behavior of a higher molecular weight noninteracting species. An immobilized monospecific antibody to l 2 removes only the l 2 polypeptide from a purified factor V preparation containing both h and l 2. Moreover, while a monospecific antibody to the h chain was able to precipitate purified radioactively labelled h chain alone or mixed with plasma, the l 2 antibody was unable to precipitate radioactively labelled h chain even after attempted recombination of the h chain with l 2 present in plasma. These studies indicate that the l 2 polypeptide is not complexed to the h chain in a purified system or in plasma and reinforce the conclusion that factor V is a single polypeptide chain uncomplexed in plasma.
ISSN:0304-4165
1872-8006
DOI:10.1016/0304-4165(82)90163-5