Destabilization of a bovine B-12 trafficking chaperone protein by oxidized form of glutathione

Title
Destabilization of a bovine B-12 trafficking chaperone protein by oxidized form of glutathione
Author(s)
김지회박지현[박지현]정진주[정진주]
Keywords
VITAMIN-B-12; STABILITY; BINDING; MMACHC
Issue Date
201204
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.420, no.3, pp.547 - 551
Abstract
The protein, bCblCpro, is a bovine B-12 trafficking chaperone involved in intracellular B-12 metabolism. bCblCpro is highly thermolabile (T-m = similar to 42 degrees C) and the reduced form of glutathione, GSH, has been found to stabilize bCblCpro as a positive regulator. In this study, we discovered that the oxidized form of glutathione, GSSG, destabilizes bCblCpro, which is derived from changes in the conformation of the protein upon GSSG binding. The binding affinity for GSSG was determined to be similar with the affinity for GSH. The AC(50) = 2.8 +/- 0.4 mM of GSSG for destabilization of bCblCpro was consistently similar with the AC(50) = 2.1 +/- 0.5 mM of GSH for stabilization of the protein. These results suggest that GSSG is a negative regulator of bCblCpro and that the molar ratio of[GSH]/[GSSG] in cells may determine the stability of the B-12 trafficking chaperone. (C) 2012 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/28637http://dx.doi.org/10.1016/j.bbrc.2012.03.031
ISSN
0006-291X
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생명공학부 > 생명공학부 > Articles
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