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J. Biol. Chem., Vol. 258, Issue 16, 9669-9675, Aug, 1983
F van der Graaf, JS Greengard, BN Bouma, DM Kerbiriou and JH Griffin
Human blood coagulation Factor XIa was reduced and alkylated under mild
conditions. The mixture containing alkylated heavy and light chains was
subjected to affinity chromatography on high Mr kininogen-Sepharose.
Alkylation experiments using [14C]iodoacetamide showed that a single
disulfide bridge between the light and heavy chains was broken to release
the light chain. The alkylated light chain (Mr = 35,000) did not bind to
high Mr kininogen-Sepharose while the heavy chain (Mr = 48,000), like
Factors XI and XIa, bound with high affinity. The isolated light chain
retained the specific amidolytic activity of native Factor XIa against the
oligopeptide substrate, pyroGlu-Pro-Arg-p- nitroanilide. Km and kcat values
for this substrate were 0.56 mM and 350 s-1 for both Factor XIa and its
light chain, and the amidolytic assay was not affected by CaCl2. However,
in clotting assays using Factor XI-deficient plasma in the presence of
kaolin, the light chain was only 1% as active as native Factor XIa. Human
coagulation Factor IX was purified and labeled with sodium [3H]borohydride
on its carbohydrate moieties. When this radiolabeled Factor IX was mixed
with Factor XIa, an excellent correlation was observed between the
appearance of Factor IXa clotting activity and tritiated activation peptide
that was soluble in cold trichloroacetic acid. Factor XIa in the presence
of 5 mM CaCl2 activated 3H-Factor IX 600 times faster than Factor XIa in
the presence of EDTA. In the absence of calcium, Factor XIa and its light
chain were equally active in activating 3H-Factor IX. In contrast to Factor
XIa, the light chain in this reaction was inhibited by calcium ions such
that, in the presence of 5 mM CaCl2, Factor XIa was 2000 times more
effective than its light chain. Neither phospholipid nor high Mr kininogen
and kaolin affected the activity of Factor XIa or its light chain in the
activation of 3H-Factor IX. These observations show that the light chain
region of Factor XIa contains the entire enzymatic active site. The heavy
chain region contains the high affinity binding site for high Mr kininogen.
Furthermore the heavy chain region of Factor XIa plays a major role in the
calcium-dependent mechanisms that contribute to the activation of Factor
IX.
Isolation and functional characterization of the active light chain of activated human blood coagulation factor XI
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