Linked Life Data

1367995

Source:http://linkedlifedata.com/resource/pubmed/id/1367995

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1992-5-4
pubmed:abstractText
An experimental study was undertaken to evaluate alternative insect cell lines to Sf9 [from Spodoptera frugiperda (fall armyworm)] for the production of recombinant proteins. Insect cell lines from two different organisms were considered: IPLB-LdEIta (LdEIta) from Lymantria dispar (gypsy moth) and IPLB-HvT1 (HvT1) from Heliothis virescens (tobacco budworm). Both LdEIta and HvT1 produced higher total activity levels of recombinant beta-galactosidase in monolayer culture than Sf9 after infection with the Autographa californica nuclear polyhedrosis virus (AcMNPV). However, only LdEIta generated a product yield (activity per milligram of total protein) which exceeded that of Sf9 (by 25%), so its growth and production characteristics were investigated in depth. LdEIta generated production levels and yields of a recombinant rotaviral protein, VP4, which exceeded those of Sf9 by 84 and 38%, respectively. In suspension culture, the LdEIta cells grew as aggregates with a doubling time several hours longer than Sf9, but the recombinant product yields of LdEIta were still higher than Sf9 by 38% in this culture environment. beta-Galactosidase expression rates and cell death rates suggested that the difference in productivity between the two hosts was due to the ability of LdEIta to survive the baculovirus infection and produce recombinant proteins longer than Sf9. The presence of LdEIta aggregates in suspension culture may be used as a method to separate live cells from dead cells, labile product, and spent medium in recombinant protein production processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
8756-7938
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
462-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Production of recombinant proteins by baculovirus-infected gypsy moth cells.
pubmed:affiliation
Department of Chemical Engineering, Johns Hopkins University, Baltimore, Maryland 21218.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.