Linked Life Data

19418270

Source:http://linkedlifedata.com/resource/pubmed/id/19418270

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-8-21
pubmed:abstractText
In this study, human alpha-1,4-N-acetylglucosaminyltransferase (alpha4GnT) fused with GFP(uv) (GFP(uv)-alpha4GnT) was expressed using both a transformed cell system and silkworm larvae. A Tn-pXgp-GFP(uv)-alpha4GnT cell line, isolated after expression vector transfection, produced 106 mU/ml of alpha4GnT activity in suspension culture. When Bombyx mori nucleopolyhedrovirus containing a GFP(uv)-alpha4GnT fusion gene (BmNPV-CP (-)/GFP(uv)-alpha4GnT) bacmid was injected into silkworm larvae, alpha4GnT activity in larval hemolymph was 352 mU/ml, which was 3.3-fold higher than that of the Tn-pXgp-GFP(uv)-alpha4GnT cell line. With human calnexin (CNX) or human immunoglobulin heavy chain-binding protein (BiP, GRP78) coexpressed under the control of the ie-2 promoter, alpha4GnT activity in larval hemolymph increased by 1.4-2.0-fold. Moreover, when BmNPV-CP (-)/GFP(uv)-alpha4GnT bacmid injection was delayed for 3 h after BmNPV-CP (-)/CNX injection, the alpha4GnT activity increased significantly to 922 mU/ml, which was 8.7-fold higher than that of the Tn-pXgp-GFP(uv)-alpha4GnT cell line. Molecular chaperone assisted-expression in silkworm larvae using the BmNPV bacmid is a promising tool for recombinant protein production. This system could lead to large-scale production of more complex recombinant proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1073-6085
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-75
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Molecular chaperone-assisted production of human alpha-1,4-N-acetylglucosaminyltransferase in silkworm larvae using recombinant BmNPV bacmids.
pubmed:affiliation
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't