A soluble cytokinin-binding protein from wheat germ that has a high affinity for a range of purine cytokinins also interacts with a variety of nonpurine compounds that can affect cytokinin-modified processes in aninal or plant cels or which bind to proteins known to interact with certain cytokinins. A variety of structuraly disprate compounds which inhibit chloroplast photosystem 11 activity (including pbenylurea, carbanilate, and alkylamino-2-chloro-syn-triazine compounds) displace High affinity cytokinin-binding proteins are present in the ribosomal and postribosomal supernatant fractions from centrifugal fractionation of wheat germ homogenates (9, 10). Fox and Erion (10) have resolved an approximately 100,000 dalton high affinity cytokinin-binding protein (CBF-1) from the ribosomal fraction from wheat germ. They have also resolved a very similar protein (probably identical to CBF-1), an approximately 30,000 dalton high affinity cytokinin-binding protein (CBF-2) and a high mol wt low affinity cytokinin-binding protein (CBF-3) from the postribosomal supernatant fraction from wheat germ (10). Polya and Davis (25) Equilibrium Dialysis. Equilibrium dialysis was performed using 10-cm-long sacs ofsize 8/32 dialysis tubing (Visking Co., Chicago) enclosing I ml of a solution containing 0.5 M (NH4)2SO4, 50 mM Tris-HCl (pH 8.0), 0.1% (v/v) 2-mercaptoethanol, and 3.6 mg CBP. Dialysis sacs were suspended in 40 ml of a solution containing 0.5 M (NH4)2S04, 50 mm Tris-HCl (pH 8.0), 0.1% (v/v)