Robot Raptor the graphics were nice.
I liked it but it had some negetive comeback on my part, Ive studied this my whole life and this is what I came up with....During growth, insects go through repeated cycles of moulting necessitating dissolution of chitin to accommodate an enlarging body. Therefore, expression of chitinase in insect larvae coincides with the moulting process and is developmentally controlled by hormones. Since chitin is a structural component in insects, its synthesis and hydrolysis are considered to be potential targets for pest management. A detailed analysis of chitin dissolution was undertaken to evaluate it as a target for a chitinase-based pesticide. We have earlier described cloning of chitinase from Helicoverpa armigera. The Helicoverpa chitinase cDNA is 2870 bp in length and contains an open reading frame of 1767 bp. The cDNA has a GC rich 5' untranslated region of 47 bp and a 3' untranslated region of 1057 bp. The sequence of translation initiation codon C A A A A T G A agrees with the Drosophila start site A A A C A T G more closely than the Kozak sequences, G C C A T G G. A polyadenylation signal sequence is present at position 2852 within the 3' UTR. The ORF encodes a polypeptide of 588 residues with a predicted molecular mass of 66 kDa. The polypeptide has two main domains, a catalytic glycosyl hydrolase conserved domain, FDGLDLDKE, and a conserved peritrophic chitin-binding domain at the C-terminus, which contained six conserved cysteines. The catalytic and chitin binding domains are held together by a proline threonine rich region which is longer in Helicoverpa than in other lepidopteran insects.
This chitinase, when expressed using a prokaryotic vector in E. coli was catalytically inefficient and hence it was cloned and expressed in Trichoplusia ni cell line using a baculovirus vector. The recombinant chitinase in T. ni cells accumulated in the culture medium and was purified by ion exchange chromatography. The purified protein displayed high catalytic activity against polymeric substrate on a glycol chitin activity gel and the fluorometric oligosacchacide substrates. The enzyme preferred trisaccharride to disaccharides on substrate and hence classified as an endochitinase, displayed bimodal pH optima at 6.0 and 7.5 and was maximally active at 45oC. Using quantitative RT-PCR chitinase transcript was found in the integument, gut, and fat bodies but was absent in haemocytes. The developmental expression of chitinase was studied in the midgut and integument by RT-PCR. The integument and midgut of larvae were collected for seven days and included moultings from fourth to fifth instar and from fifth to pupal stage. The gene-specific product was obtained at all stages under study but the relative abundance varied at each stage. A high amount of transcript was present during moulting and barely detectable levels were observed during intermoulting stages. Identical expression patterns were obtained in the integument and the midgut. Western blot analysis and integument extracts with chitinase specific antibodies showed that the enzyme was present only during moulting stages and was absent in the intermould periods. It is likely that the chitinase expression is regulated post-transcriptionally and the mRNA is translated only at the moulting stages when enzyme activity is required to degrade the cuticle
broyvms--random 
Carl Spacedew 
Ruhabs evil part 3