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

<p style="text-align: justify;">The genetic modification of Event 176 maize will not result in any change in the consumption pattern for this product. Consequently, dietary exposure to this product is anticipated to be the same as for other lines of commercially available maize.</p>

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

<p style="text-align: justify;">Results from proximate analysis, and analyses of fatty acid profiles, carotenoids, and amino acid profiles showed that Event 176 did not differ significantly from non-transformed isogenic lines, and indicated that there were no unintended effects on metabolic pathways. Comparisons of protein, fat, fibre and ash concentration of corn grain and whole plant material from Event 176 and the non-transgenic counterpart showed occasional significant differences in fat and protein content and whole plant ash content. The observed variation described was judged to be normal variation rather than due to the inserted novel trait.</p>

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

<p style="text-align: justify;">Direct toxicity studies conducted using Cry1Ab and PAT test material did not reveal any deleterious effects. The amino acid sequence of the truncated Cry1Ab protein expressed in 176 maize is closely related the sequence of the same proteins that are present in strains of <i>B. thuringiensis</i> that have been used for over 40 years as commercial organic microbial insecticides. An analysis of the amino acid sequences of the inserted Cry1Ab protein and the PAT enzyme did not show homologies with known mammalian protein toxins and they are not judged to have any potential for human toxicity.</p>

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

<p style="text-align: justify;">The truncated Cry1Ab protein and the PAT enzyme expressed in 176 corn do not possess characteristics typical of known protein allergens. There were no regions of homology when the sequences of these introduced proteins were compared to the amino acid sequences of known protein allergens. Unlike known protein allergens, both of these proteins were rapidly degraded by acid and/or enzymatic hydrolysis when exposed to simulated gastric fluids. The Cry1Ab and PAT proteins are extremely unlikely to be allergenic.</p>
