Secretion of human interleukin-2 fused with green fluorescent protein in recombinant Pichia pastoris
SCIE
SCOPUS
- Title
- Secretion of human interleukin-2 fused with green fluorescent protein in recombinant Pichia pastoris
- Authors
- Cha, HJ; Dalal, NN; Bentley, WE
- Date Issued
- 2005-07
- Publisher
- HUMANA PRESS INC
- Abstract
- Methylotrophic yeast Pichia pastoris is convenient for the expression of eukaryotic foreign proteins owing to its potential for posttranslational modifications, protein folding, and facile culturing. In this work, human interleukin (hIL)-2 was successfully produced as a secreted fusion form in recombinant P. pastoris. By employing green fluorescent protein (GFP) as a monitoring fusion partner, clear identification of fusion protein expression and quantification of intracellular hIL-2 were possible even though there was no correlation between culture supernatant fluorescence and secreted hIL-2 owing to high media interference. Importantly, by the addition of casamino acids in basal medium, we were able to enhance threefold amount of secreted hIL-2, which was present both as a fusion and as a clipped fragment.
- Keywords
- human interleukin-2; green fluorescent protein; Pichia pastoris; fusion protein; secretion; HETEROLOGOUS PROTEINS; ESCHERICHIA-COLI; FUSION PARTNER; METHYLOTROPHIC YEAST; EXPRESSION; PURIFICATION; CELLS; CONSTRUCTION; GENE
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/29614
- DOI
- 10.1007/s12010-005-0001-9
- ISSN
- 0273-2289
- Article Type
- Article
- Citation
- APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, vol. 126, no. 1, page. 1 - 11, 2005-07
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.