Abstract
Summary Based on a kinetic analysis of amino acid and protein turnover by means of compartment models the synthesis and degradation of the soluble proteins in etiolated epicotyl segments of Pisum sativum 1. as well as their dependence on the herbicice 2'-methyl-4'-chlorophenoxyacetic acid (MOPA) were quantitatively determined. The segments were incubated for 10 h in a medium containing l4O-leucine and subsequently placed in an inactive medium; the radioactivity in the soluble proteins and in the amino acid fraction was experimentally followed up for a total of 24 h. A 3-pool model in which the total measurable amino acid pool was divided into a direct precursor pool for protein synthesis and into a degradation pool was best suited to interpret the data. The turnover rate for the soluble proteins of untreated epicotyl segments was determined to be 0.058 h-1 ; at an MOPAconcentration of 10-4 M this value was nearly doubled. An increased proteolytic activity in the epicotyl segments ran parallel to the change of the turnover rate in dependence on MOP A-concentration. The heterogeneity of the soluble protein with respect to the turnover rate was investigated by means of 3H/140 double labelling for individual protein fractions separated by gel electrophoresis. The results obtained in this way are comparable with those of the investigation of the total pool turnover.
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