The development of recombinant human serum albumin

We have developed a fermentation process for recombinant human serum albumin (rHSA) production using an expression strain of the methylotrophic yeast Pichia pastoris. The high productivity of the process enables it to compete with the production of plasma derived HSA. After purification of the rHSA,...

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Bibliographic Details
Published inTherapeutic apheresis Vol. 2; no. 4; p. 257
Main Authors Kobayashi, K, Nakamura, N, Sumi, A, Ohmura, T, Yokoyama, K
Format Journal Article
LanguageEnglish
Published United States 01.11.1998
Subjects
Epitopes
Humans
Molecular Conformation
Pichia
Recombinant Proteins
Serum Albumin - chemistry
Serum Albumin - immunology
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Summary:We have developed a fermentation process for recombinant human serum albumin (rHSA) production using an expression strain of the methylotrophic yeast Pichia pastoris. The high productivity of the process enables it to compete with the production of plasma derived HSA. After purification of the rHSA, the content of yeast derived contaminants was less than 1 ng/250 mg of rHSA. The results from structural analyses suggested that purified rHSA possessed an identical conformation to plasma derived HSA. Furthermore, no neoantigenicity different from that of plasma derived HSA was observed. The efficacy and safety of rHSA were tested in clinical studies, and it was shown that there was no difference between rHSA and plasma derived HSA in a comparison study. The high efficacy of rHSA with little or no adverse reaction was confirmed in these studies.
ISSN:1091-6660
DOI:10.1111/j.1744-9987.1998.tb00118.x