Abstract
Polyclonal rabbit antiserum, raised against IAA coupled to bovine serum albumen via the indole nitrogen, was purified on a Protein A column. The immunoglobulin fraction was covalently bound to glutardialdehyde-activated silicate support and used as an immunoaffinity chromatography matrix to purify IAA in extracts from the cambial zone and shoots of Pinus sylvestris. Samples were then analysed by reverse phase HPLC with fluorescence detection. The accuracy of quantitative estimates of IAA, based on isotope dilution analyses, were verified by means of a successive approximation. The presence of IAA in the cambial tissue was further confirmed by GC/MS.
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