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kinetic constants (ka, kd)
- biac
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6 years 9 months ago #1
by biac
kinetic constants (ka, kd) was created by biac
Dear Arnould
will the kinetic constants ka, kd change if the antibody (150 KDa; higher mol wt) is used as analyte and protein X (40 KDa; low mol wt) is used as a ligand in biacore.
Will the result be same as immobilizing antibody and running protein X as analyte (which is usually the case)???
will the kinetic constants ka, kd change if the antibody (150 KDa; higher mol wt) is used as analyte and protein X (40 KDa; low mol wt) is used as a ligand in biacore.
Will the result be same as immobilizing antibody and running protein X as analyte (which is usually the case)???
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- Arnoud
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6 years 9 months ago #2
by Arnoud
Replied by Arnoud on topic kinetic constants (ka, kd)
Hi,
In principle the kinetic constants should not change if the role (ligand or analyte) of the interactants is changed.
That said, antibodies have two binding sites. Using the antibody as ligand the two binding sites are treated as independent binding sites (1:1 model). However, when the antibody is used as analyte the two binding sites are not independent anymore and this will give a bivalent analyte model.
Kind regards
Arnoud
In principle the kinetic constants should not change if the role (ligand or analyte) of the interactants is changed.
That said, antibodies have two binding sites. Using the antibody as ligand the two binding sites are treated as independent binding sites (1:1 model). However, when the antibody is used as analyte the two binding sites are not independent anymore and this will give a bivalent analyte model.
Kind regards
Arnoud
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