Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-11-4
pubmed:abstractText
The beta subunit of human chorionic gonadotropin (beta hCG), a secretory and extensively glycosylated hormone, and firefly luciferase, a non-secretory enzyme, were simultaneously synthesized in Spodoptera larvae upon infection with a dual expression recombinant baculovirus, vAc beta hCG-luc. Luciferase was retained predominantly in the body tissue while beta hCG was secreted into the hemolymph of infected larvae. Both the proteins were similar to their authentic counterparts in terms of immunoreactivity and bioactivity. The caterpillar-derived recombinant hCG exhibited reduced electrophoretic mobility on SDS-PAGE and increased biological activity as compared to the hCG expressed in insect cells in culture. The implications of using the larval system for expressing an extensively glycosylated protein are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
310
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
148-52
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Simultaneous synthesis of enzymatically active luciferase and biologically active beta subunit of human chorionic gonadotropin in caterpillars infected with a recombinant baculovirus.
pubmed:affiliation
National Institute of Immunology, Shahid Jeet Singh Marg, New Delhi, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't