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Overlapping glycosylation sequon influences the glycosylation pattern of a chimeric protein expressed in tomato leaf and callus

Paper ID Volume ID Publish Year Pages File Format Full-Text
23554 43452 2013 4 PDF Available
Title
Overlapping glycosylation sequon influences the glycosylation pattern of a chimeric protein expressed in tomato leaf and callus
Abstract

Overlapping glycosylation sequon (OGS) is composed of two overlapping N-glycosylation sequons and has been found in certain glycoproteins with pharmaceutical value. With a growing interest to produce pharmaceutical glycoproteins in plants, it is important to establish the glycosylation pattern of OGS-containing proteins expressed in varying plant tissues. Here, a chimeric OGS (NNST)-containing gene and its mutated forms (NNAT and NASNAT) were expressed in callus-derived tomato plantlets. Tissue extracts from the recombinant leaf and callus were used in immunoblotting and glycoprotein detection. We found that the glycosylation patterns of the NNST-containing chimeric protein differ from that of NNAT- and NASNAT-containing proteins.

► OGS motif in recombinant proteins is accessible. ► Glycosylation pattern of an OGS-containing protein differs between tomato tissues. ► Presence or absence of an OGS motif in plant-expressed glycoproteins is important.

Keywords
Glycosylation pattern; N-Glycosylation; Overlapping glycosylation sequon; Tomato leaf and callus
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Overlapping glycosylation sequon influences the glycosylation pattern of a chimeric protein expressed in tomato leaf and callus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 164, Issue 1, 10 March 2013, Pages 9–12
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