<p style="text-align: justify;"><b>Dietary Exposure</b></p>

<p style="text-align: justify;">Maize line DLL25 was intended mainly for use in animal feed. The major human food uses for maize are extensively processed starch and oil fractions prepared by wet or dry milling procedures and include products such as corn syrup and corn oil, bran, grits, meal and flour. Oral exposure of the introduced PAT protein, at very low levels, may occur from ingestion of processed corn products, however a lack of mammalian toxicity and the rapid digestibility of this protein has been well demonstrated. The human food uses of grain from DLL25 were not expected to be different from the uses of non-transgenic field corn varieties. As such, the dietary exposure of people to grain from DLL25 would not be different from that for other commercially available field corn varieties</p>

<p style="text-align: justify;"><b>Nutritional Data</b></p>

<p style="text-align: justify;">Forage and grain from DLL25 maize hybrids were analyzed for nutritional composition and compared to the nutritional composition of non-transgenic versions of the same maize hybrids. Proximate and amino acid analyses were performed. Small differences between DLL25 plants and their non-transgenic counterparts were occasionally observed. However, the nutrient composition of DLL25 maize fell within the range of variability for the relevant nutrients reported for maize. The use of corn products derived from DLL25 was not anticipated to have any significant impact on the nutritional quality of the food supply.</p>

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

<p style="text-align: justify;">The low potential for toxicity of the PAT protein expressed in the transgenic maize line DLL25 was investigated by searching for amino acid sequence homology with known toxins, examining its physiochemical properties and by acute oral toxicity testing in rats. A search of the GenBank database did not reveal any homologies between the deduced amino acid sequence of the PAT protein and the sequences of known protein toxins or allergens.<br />
The PAT enzyme does not possess proteolytic or heat stability typical of toxic compounds, and does not affect the metabolism of the plant. The PAT enzyme has a very specific enzymatic activity that is highly specific for glufosinate and is not expected to have any effect on metabolic pathways in the plant other than detoxification of glufosinate herbicides.</p>

<p style="text-align: justify;">An acute mouse toxicity study of bacterially-derived PAT protein was performed with no toxicity observed. Results indicated that the acute oral LD50 was estimated to be greater than 2500 mg of PAT/kg body weight. The acute oral toxicity data supported the prediction that the PAT protein was non-toxic to humans, by demonstrating a lack of mammalian toxicity</p>

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

<p style="text-align: justify;">The PAT protein does not possess characteristics typical of known protein allergens. In addition to a lack of sequence homology with known allergens, the PAT protein was rapidly degraded by simulated gastric fluids (&lt; 1 min), unlike known protein allergens. Based on these properties, it was concluded that there was little or no potential for allergenicity.</p>
