Quantitative investigation of the affinity properties of different recombinant forms of protein G by means of high-performance monolithic chromatography
- 8 March 2002
- journal article
- Published by Elsevier in Journal of Chromatography A
- Vol. 949 (1-2) , 185-193
- https://doi.org/10.1016/s0021-9673(02)00032-8
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Application of compact porous tubes for preparative isolation of clotting factor VIII from human plasmaJournal of Chromatography A, 1997
- The serum albumin‐binding domain of streptococcal protein G is a three‐helical bundle: a heteronuclear NMR studyFEBS Letters, 1996
- Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 .ANG. structure of the subtilisin-prodomain complexBiochemistry, 1995
- Rapid, automated, two-dimensional high-performance liquid chromatographic analysis of immunoglobulin G and its multimersJournal of Chromatography A, 1994
- Europium-labelled recombinant protein G: A fast and sensitive universal immunoreagent for time-resolved immunofluorometryJournal of Immunological Methods, 1993
- Determination of the solution structures of domains II and III of protein G from Streptococcus by 1H nuclear magnetic resonanceJournal of Molecular Biology, 1992
- 1.67-.ANG. X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domainBiochemistry, 1992
- A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein GScience, 1991
- Streptococcal protein G, expressed by streptococci or by Escherichia coli, has separate binding sites for human albumin and IgGMolecular Immunology, 1987
- Detection and purification of rat and goat immunoglobulin G antibodies using protein G-based solid-phase radioimmunoassaysJournal of Immunological Methods, 1986