The differential functional stability of various forms of bovine liver rhodanese
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference36 articles.
1. The covalent structure of bovine liver rhodanese. Isolation and partial structural analysis of cyanogen bromide fragements and the complete sequence of the enzyme.
2. The covalent and tertiary structure of bovine liver rhodanese
3. Structural studies of bovine liver thiosulfate sulfurtransferase II. S-carboxymethylation of the enzyme and sequence analysis of the tryptic cysteinyl peptides
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1. Inhibition of the catalytic activity of rhodanese by S-nitrosylation using nitric oxide donors;The International Journal of Biochemistry & Cell Biology;2003-12
2. Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: Possible role of a protein perselenide in a selenium delivery system;Proceedings of the National Academy of Sciences;2001-08-07
3. Mutagenic analysis of Thr-232 in rhodanese fromAzotobacter vinelandiihighlighted the differences of this prokaryotic enzyme from the known sulfurtransferases;FEBS Letters;2000-04-27
4. Alkali Metal Ions Protect Mitochondrial Rhodanese against Thermal Inactivation;Archives of Biochemistry and Biophysics;1999-01
5. Changing the Nature of the Initial Chaperonin Capture Complex Influences the Substrate Folding Efficiency;Journal of Biological Chemistry;1998-09
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