Highly efficient expression of fish growth hormone by Escherichia coli cells.

摘要

A PCR product encoding the mature segment of fish pregrowth hormone (pre-GH) was inserted into an Escherichia coli expression vector, pET, in which the ori site was replaced by that of pUC19. The yield of recombinant GH (rGH) was as high as 44 to 47% of total protein. This rGH was immunoreactive to GH antibody. After renaturation, rGH was used to inject fish with 0.1 microgram of rGH per g once every 2 weeks, and this resulted in increases in weight (65%), percent weight gain (165%), and length (22%) relative to those of an untreated control group at week 16 and onward.