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Comparison of enzymatic activities between the recombinant CHT1 proteins from the hard tick Haemaphysalis longicornis expressed in E. coli and baculovirus-mediated Sf 9 cells


Comparison of enzymatic activities between the recombinant CHT1 proteins from the hard tick Haemaphysalis longicornis expressed in E. coli and baculovirus-mediated Sf 9 cells



Korean Journal of Veterinary Research 43(1): 139-144



A chitinase cDNA named CHT1 was cloned from the hard tick Haemaphysalis longicornis and the enzymatic properties of its recombinant proteins were characterized. The CHT1 cDNA encodes 930 amino acids (aa) residues including a 22 aa putative signal peptide, with the calculated molecular mass of the putative mature protein 104 kDa. The E. coli-expressed rCHT1 exhibited weak chitinolytic activity against 4MU-(GlcNAc)3.

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