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pubmed-article:15327363pubmed:abstractTextHuman osteoprotegrin (OPG) and its truncated mutant OPG-280 and lengthened mutant OPG-Fc were constructed and successfully expressed in Trichoplusia ni cells and Bombyx mori larvae. Native SDS-PAGE and Western blot analysis revealed that OPG-Fc is present as a homodimer in Tn cells or B. mori larvae compared with OPG and OPG-280. Furthermore, the hypocalcemic effect assay showed that truncation of the C-terminal 100 residues OPG does not abolish the biological activity and Fc can be helpful in forming the OPG homodimer with improved biological activity.lld:pubmed
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pubmed-article:15327363pubmed:authorpubmed-author:LiuZhenZlld:pubmed
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pubmed-article:15327363pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15327363pubmed:year2004lld:pubmed
pubmed-article:15327363pubmed:articleTitleProduction of recombinant human osteoprotegrin from Trichoplusia ni cells and Bombyx mori larvae.lld:pubmed
pubmed-article:15327363pubmed:affiliationState Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry And Cell Biology, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China.lld:pubmed
pubmed-article:15327363pubmed:publicationTypeJournal Articlelld:pubmed