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

doi:10.1007/s12033-018-0127-y

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

Agricultural Bioresource Sciences

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15 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 language	English
Journal	Molecular Biotechnology
DOIs	https://doi.org/10.1007/s12033-018-0127-y
Publication status	Accepted/In press - Jan 1 2018

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology

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

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.",

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

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T1 - Expression, Purification, and Characterization of Recombinant Human α1-Antitrypsin Produced Using Silkworm–Baculovirus Expression System

AU - Morifuji, Yoshiki

AU - Xu, Jian

AU - Karasaki, Noriko

AU - Iiyama, Kazuhiro

AU - Morokuma, Daisuke

AU - Hino, Masato

AU - Masuda, Akitsu

AU - Yano, Takumi

AU - Mon, Hiroaki

AU - Kusakabe, Takahiro

AU - Lee, Jae Man

PY - 2018/1/1

Y1 - 2018/1/1

N2 - 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.

AB - 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.

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JF - Molecular Biotechnology

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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