Expression, Purification, and Characterization of Recombinant Human α1-Antitrypsin Produced Using Silkworm–Baculovirus Expression System

Yoshiki Morifuji, Jian Xu, Noriko Karasaki, Kazuhiro Iiyama, Daisuke Morokuma, Masato Hino, Akitsu Masuda, Takumi Yano, Hiroaki Mon, Takahiro Kusakabe, Jae Man Lee

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Human α1-antitrypsin (AAT) is the most abundant serine proteinase inhibitor (serpin) in the human plasma. Commercially available AAT for the medications of deficiency of α1-antitrypsin is mainly purified from human plasma. There is a high demand for a stable and low-cost supply of recombinant AAT (rAAT). In this study, the baculovirus expression vector system using silkworm larvae as host was employed and a large amount of highly active AAT was recovered from the silkworm serum (~ 15 mg/10 ml) with high purity. Both the enzymatic activity and stability of purified rAAT were comparable with those of commercial product. Our results provide an alternative method for mass production of the active rAAT in pharmaceutical use.

Original languageEnglish
JournalMolecular Biotechnology
DOIs
Publication statusAccepted/In press - Jan 1 2018

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Expression, Purification, and Characterization of Recombinant Human α<sub>1</sub>-Antitrypsin Produced Using Silkworm–Baculovirus Expression System'. Together they form a unique fingerprint.

Cite this