Purification of glycopeptides of human ceruloplasmin and immunoglobulin D by high-pressure liquid chromatography
- 1 July 1982
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 123 (2) , 430-437
- https://doi.org/10.1016/0003-2697(82)90468-7
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
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- Primary structure of the Fc region of human immunoglobulin D: implications for evolutionary origin and biological function.Proceedings of the National Academy of Sciences, 1981
- Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. II. Amino acid sequence of the tryptic peptides.Journal of Biological Chemistry, 1980
- Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.Journal of Biological Chemistry, 1980
- Purification and characterization of undegraded human ceruloplasminAnalytical Biochemistry, 1980
- The Use of Perfluorinated Carboxylic Acids in the Reversed-Phase HPLC of PeptidesJournal of Liquid Chromatography, 1980
- Structural studies of human IgD: Isolation by a two-step purification procedure and characterization by chemical and enzymatic fragmentationProceedings of the National Academy of Sciences, 1979
- Comparative Aspects of Glycoprotein StructureAnnual Review of Biochemistry, 1976
- The Amino‐Acid Sequences of Three Tryptic Glycopeptides from Human CeruloplasminEuropean Journal of Biochemistry, 1974