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Renaturation of Lysozyme with a Protein Disulfide Isomerase Chaperone Results in Enzyme Super Activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
21529 43226 2008 4 PDF Available
Title
Renaturation of Lysozyme with a Protein Disulfide Isomerase Chaperone Results in Enzyme Super Activity
Abstract

When the oxidative refolding of lysozyme (Lyzm) was carried out in the presence of protein disulfide isomerase (PDI) an increased refolding rate and a recovered activity exceeding 100% were reproducibly observed. The origin of this excess activity was investigated by HPLC, SDS–PAGE, and mass spectrometry and assessed using an assay for Lyzm activity. The refolding of Lyzm was achieved through the formation of PDI-Lyzm intermediates and the excess activity was derived from the nascent lysozyme released from these complexes. The released lysozyme exhibited a higher molecular activity than observed for the native protein.

Keywords
chaperoned lysozyme; lysozyme refolding; protein disulfide isomerase; super activity
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Renaturation of Lysozyme with a Protein Disulfide Isomerase Chaperone Results in Enzyme Super Activity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 106, Issue 5, November 2008, Pages 503–506
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
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Full-text PDF Download
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