Abstract
A membrane-associated indoleacetic acid (IAA)-binding site with high affinity, high specificity and finite capacity has been found in etiolated chickpea epicotyls. Dissociation constant ( K d ) and binding site concentration are 3 × 10 −7 M and 0.25 pmol/mg protein, respectively. IAA binding is optimum at pH 5.5 and 0°C. The sensitivity of specific binding to pretreatment with proteases including trypsin, sodium dodecylsulfate (SDS) and thiol-reactive agents such as parachloromercuribenzoate (PCMB) and mercuric chloride (HgCl 2) indicates that the binding moiety is a protein containing a sulfhydryl group.
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