Purification and characterization of recombinant human albumin from Hansenula polymorpha DL-1 = Hansenula polymorpha DL-1이 생산하는 재조합 알부민의 정제 및 특성

Abstract

Recombinant Human serum albumin (rHSA) was purified to near homogeneity from H. polymorpha using heat treatment, ultrafiltration and Phenyl Sepharose CL-4B and Mono Q column chromatographies with a recovery yield of 60%. The molecular weight of the purified rHSA was estimated to be about 65,000 Da by denaturing SDS-PAGE. The N-terminal amino acid sequence of the purified HSA determined by Edman degradation was turned out to be Asp-Ala-His-Lys-Ser-Glu-Val-Ala, suggesting that the rHSA expressed in H. polymorpha was efficiently secreted and correctly processed at the cleavage site of secretion signal sequence. The purified human albumin showed the pI value identical to that of authentic human serum albumin.