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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Published in | Biochimica et biophysica acta. General subjects Vol. 714; no. 3; pp. 524 - 529 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
25.02.1982
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Subjects | |
Online Access | Get full text |
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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. |
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ISSN: | 0304-4165 1872-8006 |
DOI: | 10.1016/0304-4165(82)90163-5 |