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

<p style="text-align: justify;">Grain from DBT418 is intended primarily for animal feeding. However, such field maize may be dry- or wet-milled into various processed maize products for human food use. The human food uses of grain from DBT418 plants are not expected to be different from the uses of non-transgenic field maize varieties. As such, the dietary exposure of humans to grain from DBT418 will not be different from that for other commercially available field maize varieties.</p>

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

<p style="text-align: justify;">Forage and grain from DBT418 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 DBT418 plants and their non-transgenic counterparts were occasionally observed. However, the nutrient composition of DBT418 maize falls within the range of variability for the relevant nutrients reported for maize. The use of maize products derived from DBT418 would therefore have no significant impact on the nutritional quality of the North American food supply</p>

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

<p style="text-align: justify;">The amino acid sequences of the Cry1Ac and PAT proteins were compared to databases of known protein toxins and showed no homology with known mammalian protein toxins. An acute mouse toxicity study was performed using microbially-produced, purified Cry1Ac or PAT protein. The test protein was administered at doses up to 3325 mg/kg body weight and 2500 mg/kg body weight for Cry1Ac and PAT, respectively, without any observable adverse affects. Based on the results of these studies, the acute oral LD50 was estimated to be greater than 3325 mg of Cry1Ac or 2500 mg of PAT/kg body weight.</p>

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

<p style="text-align: justify;">The likelihood of the Cry1Ac and PAT proteins being allergens was judged to be remote. No homologies were found when the deduced amino acid sequences of the introduced proteins were compared to the sequences of known allergens. In addition, the potential for allergenicity was assessed based upon the physiochemical propterties of known food allergens, such as stability to acid and/or proteolytic digestion, heat stability, glycosylation, and molecular weight. Neither the Cry1Ac protein or the PAT protein possessed these characteristics normally associated with food allergens. For example, studies demonstrated that the PAT enzyme was completely degraded within five minutes when subjected to typical mammalian gastric conditions and was thus digested as a conventional dietary protein.</p>
