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Novel site-specific immobilization of a functional protein using a preferred substrate sequence for transglutaminase 2

Paper ID Volume ID Publish Year Pages File Format Full-Text
25153 43556 2007 7 PDF Available
Title
Novel site-specific immobilization of a functional protein using a preferred substrate sequence for transglutaminase 2
Abstract

Transglutaminase (TGase) catalyzes the formation of a covalent cross-link between a peptide-bound glutamine residue and a lysine residue or primary amine. We have recently identified specific preferred sequences as glutamine-donor substrates in TGase 2 and Factor XIII reactions. By taking advantage of preference of the 12-amino acid sequence for the enzymatic reaction, an efficient immobilization method was established using two different model proteins, glutathione S-transferase (GST) and single-chain fragment antibody (scFv). Both proteins were genetically attached with the preferred substrate sequence to produce a fusion protein. Attachment of the sequence enables the recombinant proteins to act as prominent TGase-substrates and enables them to be immobilized onto chemically amine-terminated gels. Investigation of the biological activities of the two proteins demonstrated their effective immobilization in comparison with that by using a chemically immobilizing method. This established system, which we designated as Transglutaminase-mediated site-specific immobilization method (TRANSIM), would provide site-specific and biologically active conjugation between proteins and several non-protein materials.

Keywords
BSA, bovine serum albumin; CBB, Coomassie Brilliant Blue; Dansyl-Cd, monodansylcadaverine; GST, glutathione S-transferase; 6xHis, hexahistidine; NHS, N-hydroxysuccinimide; OVA, ovine albumin; scFv, single chain fragment antibody; SDS, sodium dodecyl sulfa
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Novel site-specific immobilization of a functional protein using a preferred substrate sequence for transglutaminase 2
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 131, Issue 2, 31 August 2007, Pages 121–127
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us