High Expression and
Purification of Recombinant Human Serum Albumin from Pichia
pastoris
QIU Rong-De, LI Shi-Yun, CHEN Jun-Gang, WU Xiang-Fu, YUAN
Zhong-Yi*
( Shanghai Institute of Biochemistry, the Chinese Academy of Science,
Shanghai 200031, China )
Abstract Recombinant
human serum albumin (rHSA) was produced in methylotrophic yeast Pichia
pastoris. By optimization of expression, about 150 mg/L of rHSA was obtained
from broth of Pichia pastoris GS115/HSA (his+MutS) supernatant. The rHSA was
isolated and purified by hollow-fiber ultrafiltration, Phenyl-Sepharose
hydrophobic chromatography and antibody-immunoadsorbent chromatography.
Finally, rHSA was purified to electrophoretic purity.
Key Words rHSA； Pichia pastoris； gene expression； isolation and
purification
Received: August 18,
1999 Accepted: September 13, 1999
* Corresponding author: Tel, 86-21-64374430; Fax, 86-21-64338357; e-mail, [email protected]