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. Author manuscript; available in PMC: 2007 Oct 18.
Published in final edited form as: J Biol Chem. 2005 May 19;280(31):28711–28720. doi: 10.1074/jbc.M500478200

TABLE II.

Assembly of vitronectin and PAI-1 into intermediate and higher order complexes. Ranges in s values were defined for integration according to the criteria outlined in Table I, with species sedimenting with s values in the range from 1 to 5 S representing free vitronectin and PAI-1, species with s values in the range from 5.1 to 7.4 S representing intermediate 1:1 and 2:1 complexes, and species sedimenting with s values greater than 7.5 S representing higher order complexes of vitronectin and PAI-1.

Protein samples Protein concentrations Unbound proteins (fraction in s range from 1to5 S)a Intermediate complexes (fraction in s range from 5.1 to 7.4 S)a Higher order complexes (fraction in s range from 7.5 to 25 S)a
% % %
Vitronectin + wild-type PAI-1 8 μM vitronectin 8 μM PAI-1b 26 24 50
Vitronectin + wild-type PAI-1 3.2 μM vitronectin 3.2 μM PAI-1b 25 45 30
Vitronectin + wild-type PAI-1 1.6 μM vitronectin 1.6 μM PAI-1b 30 64 6
Vitronectin + Y175F PAI-1 3.3 μM vitronectin 3.3 μM PAI-1 25 34 41
Vitronectin + PAI-1R 3.3 μM vitronectin 3.3 μM PAI-1 20 40 40
a

Sedimentation data were evaluated as c(s) profiles, and data were integrated using SEDFIT to determine the relative amounts of various PAI-1-vitronectin complexes formed in the three mixtures. Values were normalized by dividing the integrated values by the total loading signal in fringes and multiplying by 100 to obtain a percentage of the various species formed. Errors are ± 5%.

b

c(s) distributions of complexes with s values >5 S for the three concentrations of vitronectin and wild-type PAI-1 samples are shown in Fig. 3, BD. Free proteins that sediment in the 1—5 S range are not shown in the figure, but the integrations over this s range are shown here.