1. Molecular Cloning and Analysis of theTryptophan oxygenaseGene in the Silkworm,Bombyx mori
- Author
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Shen WeiFeng, Meng ZhiQi, Weng Hongbiao, Niu Baolong, Liu Yan, and He Lihua
- Subjects
Molecular Sequence Data ,Molecular cloning ,Gene Expression Regulation, Enzymologic ,Protein Structure, Secondary ,Article ,Bombycidae ,eye pigmentation ,vermilion gene ,Bombyx mori ,Complementary DNA ,Animals ,Amino Acid Sequence ,Cloning, Molecular ,Peptide sequence ,Gene ,Phylogeny ,Base Sequence ,Molecular mass ,biology ,Gene Expression Profiling ,fungi ,General Medicine ,Bombyx ,biology.organism_classification ,Eye pigmentation ,Molecular biology ,Tryptophan Oxygenase ,Lepidoptera ,Biochemistry ,Insect Science ,Sequence Alignment - Abstract
A Bombyx mori L. (Lepidoptera: Bombycidae) gene encoding tryptophan oxygenase has been molecularly cloned and analyzed. The tryptophan oxygenase cDNA had 1374 nucleotides that encoded a 401 amino acid protein with an estimated molecular mass of 46.47 kDa and a PI of 5.88. RT-PCR analysis showed that the B. mori tryptophan oxygenase gene was transcribed in all examined stages. Tryptophan oxygenase proteins are relatively well conserved among different orders of arthropods.
- Published
- 2008