Purification and identification of recombinant hirudin and its degradation products expressed in Pichia pastoris |
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Authors: | Zhou Wei-Bin Zhang Yuan-Xing |
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Institution: | State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, P.R. China. |
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Abstract: | The purification and identification of recombinant hirudin (r-hirudin) (rHV2-Lys47) and its several C-terminal proteolytic degradation derivatives, produced by Pichia pastoris, were described. The high-purity rHV2-Lys47 of above 99% and its three degradation products were obtained by a straightforward two-step chromatography procedure, a combination of cation exchange and reverse phase chromatography, with a recovery yield of 74% for hirudin. The purified rHV2 had the predicted N-terminal amino acid sequence and the derivatives were the degradation products of hirudin, short of one to three amino acid residues at C-terminal. |
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