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Functional Recombinants Designed from a Fetuin/Asialofetuin-Specific Marine Algal Lectin, Rhodobindin
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Plant lectins have attracted much attention for biomedical applications including targeted drug delivery system and therapy against tumors and microbial infections. The main problem of using lectins as a biomedical tool is a batch-to-batch variation in isoforms content. The production of lectins using recombination tools has the advantage of obtaining high amounts of proteins with more precise properties, but there are only a handful of functional recombinant lectins presently available. A fetuin/asialo-fetuin specific lectin, Rhodobindin, has unique tandem repeats structure which makes it useful in exploiting for recombinant lectin. We developed three functional recombinant lectins using E. coli expression system: one from full cDNA sequence and two from fragmentary sequences of Rhodobindin. Hemagglutinating activity and solubility of the recombinant lectins were highest at OD 0.7 cell concentration at 20 °C. The optimized process developed in this study was suitable for the quality-controlled production of high amounts of soluble recombinant lectins.
Title: Functional Recombinants Designed from a Fetuin/Asialofetuin-Specific Marine Algal Lectin, Rhodobindin
Description:
Plant lectins have attracted much attention for biomedical applications including targeted drug delivery system and therapy against tumors and microbial infections.
The main problem of using lectins as a biomedical tool is a batch-to-batch variation in isoforms content.
The production of lectins using recombination tools has the advantage of obtaining high amounts of proteins with more precise properties, but there are only a handful of functional recombinant lectins presently available.
A fetuin/asialo-fetuin specific lectin, Rhodobindin, has unique tandem repeats structure which makes it useful in exploiting for recombinant lectin.
We developed three functional recombinant lectins using E.
coli expression system: one from full cDNA sequence and two from fragmentary sequences of Rhodobindin.
Hemagglutinating activity and solubility of the recombinant lectins were highest at OD 0.
7 cell concentration at 20 °C.
The optimized process developed in this study was suitable for the quality-controlled production of high amounts of soluble recombinant lectins.
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