AI Article Synopsis
- Recombinant human midkine (rh-midkine) was successfully expressed using the AOX1 gene promoter in the yeast Pichia pastoris, resulting in approximately 640 mg being secreted per liter of fermentation.
- The protein processing was efficient, with no O-mannosylation observed in the purified product, but only 30% of the rh-midkine was fully intact; the rest had lost some amino acids from the amino-termini due to proteolysis.
- Despite these truncations, the modified versions of midkine were still effective in promoting CHO cell proliferation, similar to the original rh-midkine.
Article Abstract
Recombinant human midkine (rh-midkine) was expressed under the control of the AOX1 gene promoter in Pichiapastoris. Approximately 640 mg of rh-midkine was secreted into one liter of medium of the high cell-density fermentation. The protein processing of the rh-midkine was done efficiently and correctly in P. pastoris, and O-mannosylation was not detected in the purified rh-midkine. However, only about 30% of the purified rh-midkine was intact. The other ones lost 5-12 amino acid residues from the amino-termini, provably by proteolysis. Even the mixture of these truncated midkines could promote CHO cell proliferation as well as the authentic rh-midkine.
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| http://dx.doi.org/10.1271/bbb.66.1295 | DOI Listing |
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