High Expression and Purification of Amino-Terminal Fragment of Human Amyloid Precursor Protein in <i>Pichia pastoris</i> and Partial Analysis of Its Properties

<table>Purified recombinant N-APP by Sephacryl S-200 high resolution chromatography. (a) Profile of gel filtration of the fractions from the Q Sepharose fast flow chromatography. The arrow indicates the purified protein eluting peak (13.3 mL) which corresponds to the 6th, 7th, 8th, 9th, and 10th collection tube; (b) SDS-PAGE analysis of the purified N-APP after gel filtration. M: protein marker; lanes 6–10: the eluting fraction which corresponds to the 6th, 7th, 8th, 9th, and 10th collection tube.</table>

BioMed Research International

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Figure 4: High Expression and Purification of Amino-Terminal Fragment of Human Amyloid Precursor Protein in <i>Pichia pastoris</i> and Partial Analysis of Its Properties 

Figure 4 | High Expression and Purification of Amino-Terminal Fragment of Human Amyloid Precursor Protein in Pichia pastoris and Partial Analysis of Its Properties 