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Development of a method for the efficient release of N-glycans from glycoproteins generating native deglycosylated proteins

Paper ID Volume ID Publish Year Pages File Format Full-Text
17434 42668 2012 4 PDF Available
Title
Development of a method for the efficient release of N-glycans from glycoproteins generating native deglycosylated proteins
Abstract

In many cases, it is desirable to maintain the native status of the target glycoproteins when they are deglycosylated. However, most conventional deglycosylation process often causes the irreversible denaturation of the target glycoproteins. In the present study, we developed a deglycosylation method that could obtain the native deglycosylated proteins employing Png1p-ΔH1, which was confirmed to tolerate high concentration of dithiothreitol (DTT). To prove this process, ribonuclease B (RNase B) and Yeast carboxypeptidase (CPY) were employed as the targeting glycoproteins. Our results confirmed that both of them could be completely deglycosylated in the presence of high concentration DTT and could be refolded when DTT was removed. The circular dichroism spectroscopy (CD) measurement of refolded CPY and RNase B indicated that the structure of deglycosylated proteins had recovered their native status. This method offers the possibility of efficiently releasing N-linked glycans from glycoproteins and obtaining the native target proteins.

► Develope a deglycosylation method that can obtain the native deglycosylated proteins. ► Ribonuclease B and yeast carboxypeptidase were employed as the targeting glycoprotein. ► Substrates completely deglycosylate in the presence of high concentration DTT. ► Deglycosylated substrates could be refolded when DTT was removed. ► The CD measurement indicates the deglycosylated proteins recovered native status.

Keywords
Png1p-ΔH1; Dithiothreitol; Deglycosylation; Refolding; Native deglycosylated proteins
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Development of a method for the efficient release of N-glycans from glycoproteins generating native deglycosylated proteins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 51, Issue 3, 10 August 2012, Pages 139–142
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