Multimerization of bovine Thyroglobulin, partially unfolded or partially unfolded/reduced; Involvement of protein disulfide isomerase and glutathionylated disulfide linkage-Reference-Cited by-同舟云学术

Multimerization of bovine Thyroglobulin, partially unfolded or partially unfolded/reduced; Involvement of protein disulfide isomerase and glutathionylated disulfide linkage

Published:2004-12 Issue:12 Volume:27 Page:1275-1283
ISSN:0253-6269
Container-title:Archives of Pharmacal Research
language:en
Short-container-title:Arch Pharm Res

Author:

Liu Xi-Wen,Sok Dai-Eun

Publisher

Springer Science and Business Media LLC

Subject

Organic Chemistry,Drug Discovery,Molecular Medicine

Link

http://link.springer.com/content/pdf/10.1007/BF02975894.pdf

Reference29 articles.

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2. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem., 72, 248–254 (1976).

3. Chernoff, S. B. and Rawitch, A. B., Thyroglobulin structurefunction. Isolation and characterization of a thyroxinecontaining polypeptide from bovine thyroglobulin.J. Biol. Chem., 256, 9425–9430 (1981).

4. Cuozzo, J. W. and Kaiser, C. A., Competition between glutathione and protein thiols for disulphide-bond formation.Nature Cell Biol., 1, 130–135 (1999).

5. Darby, N. J., Freedman, R. B., and Creghton, T. E., Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide.Biochemistry, 33, 7937–7947 (1994).

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