Abstract
The interaction between recombinantStrongylocentrotus purpuratussperm bindin and a recombinant fragment of the putative egg bindin receptor of the same species was measuredin vitro.In solution these molecules interact with simple bimolecular kinetics, displaying an equilibrium dissociation constant of about 0.1 μM.Thus, as implied by many observationsin vivoandin vitro,bindin and the putative egg receptor display a specific affinity for one another.
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