C-terminal truncation of a bovine B-12 trafficking chaperone enhances the sensitivity of the glutathione-regulated thermostability

Title
C-terminal truncation of a bovine B-12 trafficking chaperone enhances the sensitivity of the glutathione-regulated thermostability
Author(s)
김지회정진주박지현이동연
Keywords
PROTEIN STABILITY; VITAMIN-B-12; MMACHC; BINDING
Issue Date
201303
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Citation
BMB REPORTS, v.46, no.3, pp.169 - 174
Abstract
The human B-12 trafficking chaperone hCblC is well conserved in mammals and non-mammalian eukaryotes. However, the C-terminal similar to 40 amino acids of hCblC vary significantly and are predicted to be deleted by alternative splicing of the encoding gene. In this study, we examined the thermostability of the bovine CblC truncated at the C-terminal variable region (t-bCblC) and its regulation by glutathione. t-bCblC is highly thermolabile (T-m = similar to 42 degrees C) similar to the full-length protein (f-bCblC). However, t-bCblC is stabilized to a greater extent than f-bCblC by binding of reduced glutathione (GSH) with increased sensitivity to GSH. In addition, binding of oxidized glutathione (GSSG) destabilizes t-bCblC to a greater extent and with increased sensitivity as compared to f-bCblC. These results indicate that t-bCblC is a more sensitive form to be regulated by glutathione than the full-length form of the protein. [BMB Reports 2013; 46(3): 169-174]
URI
http://hdl.handle.net/YU.REPOSITORY/26227http://dx.doi.org/10.5483/BMBRep.2013.46.3.158
ISSN
1976-6696
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생명공학부 > 생명공학부 > Articles
공과대학 > 기계공학부 > Articles
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