Abstract:
:The constant (CL) fragment of the immunoglobulin light chain contains only one intrachain disulfide bond buried in the interior of the molecule. The kinetics of reduction with dithiothreitol of the disulfide bond were studied at various concentrations of guanidine hydrochloride at pH 8.0 and 25 degrees C. It was found that the disulfide bond is reduced even in the absence of guanidine hydrochloride. The results of the reduction kinetics were compared with those of the unfolding and refolding kinetics of the CL fragment previously reported [Goto, Y., & Hamaguchi, K. (1982) J. Mol. Biol. 156, 891-910]. It was shown that the reduction of the disulfide bond proceeds through a species with a conformation very similar to that of the fully unfolded one and that the CL fragment undergoes global unfolding transition even in water.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kikuchi H,Goto Y,Hamaguchi Kdoi
10.1021/bi00356a026subject
Has Abstractpub_date
1986-04-22 00:00:00pages
2009-13issue
8eissn
0006-2960issn
1520-4995journal_volume
25pub_type
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