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Efficient production of human Fas receptor extracellular domain-human IgG1 heavy chain Fc domain fusion protein using baculovirus/silkworm expression system.

Abstract：

:The fusion protein consisting of human Fas receptor extracellular domain and human IgG1 heavy chain Fc domain (hFasRECD-Fc) is a medically important protein that potentially has therapeutic uses. The fusion gene composed of a synthetic human Fas receptor extracellular domain gene and the cDNA encoding human IgG1 heavy chain Fc domain was investigated on the secretory expression using two baculovirus systems which employed either Spodoptera frugiperda 9 (Sf9) cell line or Bombyx mori (silkworm) larvae as the host organism. Both expression systems produced the functional hFasRECD-Fc as a dimer molecule linked by disulfide bridges. The secretion level per unit volume was much higher in the case of silkworm larvae as compared to Sf9 cell line, and was estimated to be more than 150 times. A substantially pure hFasRECD-Fc sample from silkworm larvae was obtained by single step Protein G-agarose affinity column chromatography. The affinity purified sample was further fractionated by anion-exchange chromatography with the final purification yield of 22.5 mg from 26 ml hemolymph. The hFasRECD-Fc from silkworm larvae and the tag-free human Fas ligand extracellular domain derivative from Pichia pastoris formed a stable complex in solution, which was verified by size-exclusion chromatography. This study demonstrated that the baculovirus/silkworm expression system provided the means for efficient production of highly pure hFasRECD-Fc with functional activity.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Muraki M,Honda S

doi

10.1016/j.pep.2010.05.007

subject

Has Abstract

pub_date

2010-10-01 00:00:00

pages

209-16

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(10)00155-5

journal_volume

73

pub_type

杂志文章

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