Biology Reference
In-Depth Information
5.
A concentration of ligand in the range 0.1-10
g/mL should give a good response
if the interaction is of high to moderate affinity. Other reagents (e.g., MAbs,
peptides, or synthetic compounds) can be added simultaneously with the ligand
at this stage to test for their effects on binding.
µ
References
1. Charo, I. F., Nannizzi, L., Phillips, D. R., Hsu, M. A., and Scarborough, R. M.
(1991) Inhibition of fibrinogen binding to GP IIb-IIIa by a GP IIIa peptide.
J.
Biol. Chem.
266,
1415-1421.
2. Mould, A. P., Akiyama, S. K., and Humphries, M. J. (1995) Regulation of integrin
α
1-fibronectin interactions by divalent cations. Evidence for distinct classes of
binding sites for Mn
2+
, Mg
2+
, and Ca
2+
.
J. Biol. Chem.
270,
26,270-26,277.
3. Mould, A. P., Garratt, A. N., Askari, J. A., Akiyama, S. K., and Humphries, M. J.
(1995) Identification of a novel monoclonal antibody that recognises a ligand-
induced binding site epitope on the
5
β
1 subunit. FEBS Lett.
363,
118-122.
4. Mould, A. P., Akiyama, S. K., and Humphries, M. J. (1996) The inhibitory anti-
β
β
1 integrin monoclonal antibody 13 recognises an epitope that is attenuated by
ligand occupancy. Evidence for allosteric inhibition of integrin function.
J. Biol.
Chem.
271,
20,365-20,374.
5. Mould, A. P., Askari, J. A., Aota, S., Yamada, K., Irie, A., Takada, Y., et al.
(1997) Defining the topology of integrin
α
5
β
1-fibronectin interactions using
1 monoclonal antibodies. Evidence that the synergy
sequence of fibronectin is recognised by the amino-terminal repeats of the
inhibitory anti-
α
5 and anti-
β
α
5
subunit.
J. Biol. Chem.
272,
17,283-17,292.
6. Mould, A. P. (1998) Analyzing integrin-dependent adhesion unit 9-4, in
Current
Protocols in Cell Biology
(Yamada, K. M. and Lipincott-Schwartz, J., eds.),
Wiley, New York.
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