Abstract:
:BmK ITa1 cDNA was cloned and highly expressed in E. coli and insect cell. SDS-PAGE and western blot analysis revealed that subunit molecular weight of expression products is about 40 kDa and 10 kDa respectively. The expression product purified by a Ni(2+)-IDA-sepharose 6B column was toxic for insect, which indicated that it was biologically activity. Furthermore, Quantitative estimation show that the biological activity of recombinant BmK ITa1 from Tn cells was more powerful than from E. coli.
journal_name
Protein Pept Lettjournal_title
Protein and peptide lettersauthors
Liu Z,Yang GZ,Chi CW,Wu XFdoi
10.2174/0929866023408472subject
Has Abstractpub_date
2002-10-01 00:00:00pages
419-26issue
5eissn
0929-8665issn
1875-5305journal_volume
9pub_type
杂志文章abstract::Classification of newly determined protein structures is important in understanding their function and mechanism of action. Currently available methods employ a global structure alignment strategy and are computationally expensive. We propose a two-step methodology with a quick screen to significantly reduce the numbe...
journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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