A study of peroxidase synthesis by means of double labelling and affinity chromatography

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Abstract
Peanut cells in suspension culture were incubated with [3H]leucine and [14C]5-aminolevulinic acid for 16 h. The cells were broken and extracted with a neutral buffer and a high-salt solution. Subsequently, the isolated fractions were passed through a Concanavaline A Sepharose column. It was observed that not all of the peroxidase (EC 1.11.1.7) activity was retained on the affinity column. However, the retained fraction, particularly that obtained from the high-salt extract, showed a single anionic protein with an Rf of 0.12 and with peroxidase activity. Moreover this fraction and protein has a high 14C/3H ratio (0.8) compared with the other fractions. The low specific radioactivity of this protein and its ionic bonding suggest that it may exist as a pool in the cell wall.

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