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

被引:16
|
作者
Morifuji, Yoshiki [1 ]
Xu, Jian [1 ]
Karasaki, Noriko [1 ]
Iiyama, Kazuhiro [2 ]
Morokuma, Daisuke [1 ]
Hino, Masato [1 ]
Masuda, Akitsu [1 ]
Yano, Takumi [1 ]
Mon, Hiroaki [1 ]
Kusakabe, Takahiro [1 ]
Lee, Jae Man [1 ]
机构
[1] Kyushu Univ, Grad Sch Bioresource & Bioenvironm Sci, Lab Insect Genome Sci, Higashi Ku, Hakozaki 6-10-1, Fukuoka, Fukuoka 8128581, Japan
[2] Kyushu Univ, Grad Sch Bioresource & Bioenvironm Sci, Plant Pathol Lab, Higashi Ku, Hakozaki 6-10-1, Fukuoka, Fukuoka 8128581, Japan
关键词
Baculovirus expression vector system; Serpin; alpha(1)-Antitrypsin; Recombinant protein; Silkworm; HUMAN ALPHA(1)-PROTEINASE INHIBITOR; HUMAN ALPHA-1-ANTITRYPSIN; HUMAN PLASMA; BOMBYX-MORI; PROTEIN; YIELD;
D O I
10.1007/s12033-018-0127-y
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Human alpha(1)-antitrypsin (AAT) is the most abundant serine proteinase inhibitor (serpin) in the human plasma. Commercially available AAT for the medications of deficiency of alpha(1)-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 (similar to 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.
引用
收藏
页码:924 / 934
页数:11
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