Covalent chromatography as a means of isolating thiol peptides from large proteins
- 1 October 1981
- journal article
- research article
- Published by Elsevier in Journal of Chromatography A
- Vol. 215 (1-3), 341-350
- https://doi.org/10.1016/s0021-9673(00)81413-2
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Complete amino acid sequence of a 50,000-dalton fragment of human ceruloplasmin.Proceedings of the National Academy of Sciences, 1981
- Complete amino acid sequence of a histidine-rich proteolytic fragment of human ceruloplasmin.Proceedings of the National Academy of Sciences, 1979
- Specific isolation of cysteine peptides by covalent chromatography on thiol agarose derivativesFEBS Letters, 1977
- Reinvestigation of some physicochemical and chemical properties of human ceruloplasmin (ferroxidase)Biochemistry, 1976
- A reporter group delivery system with both absolute and selective specificity for thiol groups and an improved fluorescent probe containing the 7-nitrobenzo-2-oxa-1,3-diazole moietyBiochemical Journal, 1975
- A rapid and specific method for isolation of thiol-containing peptides from large proteins by thiol-disulfide exchange on a solid support.Proceedings of the National Academy of Sciences, 1975
- Reactivities of the cysteinyl residues of human ceruloplasmin (ferroxidase)FEBS Letters, 1975
- Covalent chromatography. Preparation of fully active papain from dried papaya latexBiochemical Journal, 1973
- Evidence for proteolytic fragments in commercial samples of human ceruloplasminFEBS Letters, 1971
- Sulfhydryl Groups in Human CeruloplasminEuropean Journal of Biochemistry, 1969