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Journal of Biomedicine and Biotechnology
Volume 2010 (2010), Article ID 306462, 6 pages
Research Article

In Vivo Bioassay of Recombinant Human Growth Hormone Synthesized in B. mori Pupae

1College of Life Sciences, Zhejiang University, Hangzhou 310058, China
2Institute of Biochemistry, Zhejiang Sci-Tech University, Hangzhou 310018, China
3School of Applied Technology, Zhejiang Economic & Trade Polytechnic, Hangzhou 310018, China

Received 26 July 2009; Revised 13 December 2009; Accepted 15 January 2010

Academic Editor: Mark Smith

Copyright © 2010 Hanglian Lan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The human growth hormone (hGH) has been expressed in prokaryotic expression system with low bioactivity previously. Then the effective B. mori baculovirus system was employed to express hGH identical to mature hGH successfully in larvae, but the expression level was still limited. In this work, the hGH was expressed in B. mori pupae by baculovirus system. Quantification of recombinant hGH protein (BmrhGH) showed that the expression of BmrhGH reached the level of approximately 890  πœ‡ g/mL pupae supernatant solution, which was five times more than the level using larvae. Furthermore, Animals were gavaged with BmrhGH at the dose of 4.5 mg/rat.day, and the body weight gain (BWG) of treated group had a significant difference ( 𝑃 < . 0 1 ) compared with the control group. The other two parameters of liver weight and epiphyseal width were also found to be different between the two groups ( 𝑃 < . 0 5 ). The results suggested that BmrhGH might be used as a protein drug by oral administration.