[RASMB] Re: Fab - protein antigen association

[A Keeble]

A good starting point would be to look at the literature involving hen egg 
white lysozyme (HEL) as a lot of the basic work on antibody-antigen binding 
has been carried out on this (by R. A. Mariuzza and others). A couple of 
studies (particularly from M. G. Gore's lab) have recently looked at the 
kinetics of the Ig binding domain of protein L binding to kappa light 
chains.
    Fundamentally, increasing salt usually slows association rate constants 
to the value due to hydrophobic interactions i.e., ~ 100,000 M-1 s-1 so you 
would perhaps expect a similar thing to be true here. S.J. Smith-Gill has 
observed that protein recognition involving HEL antibodies involves a lot 
of electrostatic interactions in line with this. However Xavier KA & 
Willson RC. (Biophys J. 1998 Apr;74(4):2036-45.) studying HEL binding to 
the HyHEL-5 and HyHEL-10 antibodies did not find much of a salt dependence 
on the association kinetics.
      I hope this helps a little

Anthony Keeble





> 
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> Today's Topics:
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>    1. Fab - protein antigen association (Allen Minton)
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> --__--__--
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> Message: 1
> Date: Mon, 08 Mar 2004 09:45:44 -0500
> To: rasmb at alpha.bbri.org
> From: Allen Minton <minton at helix.nih.gov>
> Subject: [RASMB] Fab - protein antigen association
> 
> Hello RASMBers -
> 
> Can anyone point me toward quantitative studies of associations of 
> monoclonal Fab fragments with the corresponding protein antigen?  I am 
> particularly interested in the dependence of rates and equilibria upon 
> ionic strength.
> 
> Thanks,
> Allen Minton
> 
> 
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