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Title of Journal: Appl Biochem Biotechnol

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Abbravation: Applied Biochemistry and Biotechnology

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Springer US

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DOI

10.1007/s10694-010-0142-4

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ISSN

1559-0291

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Expression Purification and Characterization of

Authors: Takumi Mitsudome Jian Xu Yudai Nagata Atsushi Masuda Kazuhiro Iiyama Daisuke Morokuma Zhiqing Li Hiroaki Mon Jae Man Lee Takahiro Kusakabe
Publish Date: 2014/03/06
Volume: 172, Issue: 8, Pages: 3978-3988
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Abstract

EndoβNacetylglucosaminidase Endo H from Streptomyces plicatus hydrolyzes the core diGlcNAc units of asparaginelinked oligosaccharides and is regarded as an important tool for glycobiology research In the present study we established a largescale system to produce secreted Endo H using a silkwormbaculovirus expression system silkwormBES The recombinant Endo H purified from silkworm hemolymph had activity comparable to that from recombinant Escherichia coli As well as its wellcharacterized substrate RNase B the Endo H from silkwormBES was able to deglycosylate the highmannose glycoproteins from silkworm hemolymph Interestingly the secretion amount of recombinant Endo H was significantly varied among the different silkworm strains which could provide valuable information for largerscale protein productions from silkwormBESThe NIASBmoyanagi2 cell line for propagation of recombinant BmNPVs was kindly provided by Dr Imanishi National Institute of Agrobiological Sciences Japan We also thank Dr Chisa Aoki Kyushu University Graduate School for providing the Bme21 cell line for the expression of recombinant protein The MALDI TOF MS was kindly supported and analyzed by Center for Advanced Instrumental and Educational Supports Faculty of Agriculture Kyushu University

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