<p style="text-align: justify;"><b>Nutritional Data (Livestock Feed Purposes)</b></p>

<p style="text-align: justify;">Data on fatty acid profiles, protein content, amino acid composition, crude fibre, ash, phytate, and moisture content were provided for grain samples from lines CL121, CL141, and CFX51, and five commercial varieties grown in three locations in the United States. Comparisons of these parameters between the herbicide-tolerant lines and conventional commercial varieties did not reveal any biologically significant differences.</p>

<p style="text-align: justify;"><b>Toxicity and Allergenicity</b></p>

<p style="text-align: justify;">The single amino acid change within the native ALS enzyme was not anticipated to have any effect on the potential toxicity or allergenicity of this protein. The unmodified form of this enzyme does not display amino acid sequence homology with known protein toxins or allergens. Studies on the modified ALS protein isolated from the original mutant line, 93AS3510, demonstrated that it was rapidly inactivated by heat (1 minute at 100&deg;C) and was completely degraded within 5 minutes of treatment with trypsin. Susceptibility to heat inactivation and sensitivity to proteolytic degradation are not characteristics of known protein toxins or allergens.</p>

<p style="text-align: justify;">Measurements of the concentrations of normally occurring rice antinutritional factors (<i>e.g.</i>, phytic acid, trypsin inhibitor, and lectin) did not reveal any differences between these herbicide-tolerant lines and five conventional commercial rice varieties. For all of these varieties, the concentrations of trypsin inhibitor and hemagglutinins (i.e. lectins) were below the threshold of detection.</p>
