Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Czeslaw Radziejewski"'
Autor:
Jianwen Xu, Siew Leong Chan, Czeslaw Radziejewski, Chaohong Sun, Andrew Namanja, Peter M. Ihnat, Chelsea Son, Andrew M. Petros
Publikováno v:
Journal of pharmaceutical sciences. 110(12)
The purpose of this investigation was to highlight the utility of nuclear magnetic resonance (NMR) as a multi-attribute method for the characterization of therapeutic antibodies. In this case study, we compared results from isothermal chemical denatu
Autor:
Ivan Correia, Siew Leong Chan, Jian Shi, Paul Matsudaira, Czeslaw Radziejewski, Chloe Ng, Bich Tran
Publikováno v:
Protein Science. 26:2392-2398
Adalimumab and Infliximab are recombinant IgG1 monoclonal antibodies (mAbs) that bind and neutralize human tumor necrosis factor alpha (TNFα). TNFα forms a stable homotrimer with unique surface-exposed sites for Adalimumab, Infliximab, and TNF rece
Autor:
Clarissa G. Jakob, Bridget Carragher, Ivan Correia, Randall E. Burton, Joyce J. Sung, Tariq Ghayur, Czeslaw Radziejewski
Publikováno v:
mAbs. 5:364-372
A dual-specific, tetravalent immunoglobulin G-like molecule, termed dual variable domain immunoglobulin (DVD-Ig™), is engineered to block two targets. Flexibility modulates Fc receptor and complement binding, but could result in undesirable cross-l
Autor:
Taro Fujimori, Aima Acquah, Leslie Alessandri, David Ouellette, Czeslaw Radziejewski, Mathew Rieser, Ivan Correia, Mary Saltarelli, David LeBlond
Publikováno v:
mAbs
The role of Fc glycans on clearance of IgG molecule has been examined by various groups in experiments where specific glycans have been enriched or the entire spectrum of glycans was studied after administration in pre-clinical or clinical pharmacoki
Publikováno v:
Analytical Biochemistry. 408:277-283
The light chain cysteine residue that forms an interchain disulfide bond with the cysteine residue in the heavy chain in IgG1κ is the last amino acid. The cysteine residue is followed by a serine residue in IgG1λ. Effect of the serine residue on th
Publikováno v:
Analytical Chemistry. 82:5219-5226
One of the basic structural features of human IgG1 is the arrangement of the disulfide bond structure, 4 inter chain disulfide bonds in the hinge region and 12 intra chain disulfide bonds associated with twelve individual domains. Disulfide bond stru
Autor:
Leslie Alessandri, Christine Grinnell, Czeslaw Radziejewski, Edit Tarcsa, Ivan Correia, David Ouellette, Adam T Chin
Publikováno v:
Analytical Biochemistry. 397:37-47
Recombinant monoclonal antibodies undergo extensive posttranslational modifications. In this article, we characterize major modifications, separated by cation exchange chromatography, on an immunoglobulin G1 (IgG1) monoclonal antibody (mAb). We found
Autor:
David Ouellette, Aima Aikhoje, Ivan Correia, Reema Piparia, Leslie Alessandri, Czeslaw Radziejewski, Adam T Chin
Publikováno v:
Analytical Biochemistry. 389:107-117
Monoclonal antibodies in liquid formulation undergo nonenzymatic hydrolysis when stored at 5 degrees C for extended periods. This hydrolysis is enhanced at extreme pH and high temperature. In this study we discover that iron in the presence of histid
Publikováno v:
Rapid Communications in Mass Spectrometry. 22:1-10
Nitration of a recombinant human monoclonal antibody was carried out in vitro by incubating the antibody with the nitrating reagent tetranitromethane (TNM). The susceptible sites of nitration were identified using high-performance liquid chromatograp
Autor:
Patrick Hossler, Yu Zhou, Chris Chumsae, Sean McDermott, Czeslaw Radziejewski, Haly Raharimampionona, Christopher Racicot, Zhaohui Sunny Zhou
Publikováno v:
Analytical chemistry. 87(15)
With the advent of new initiatives to develop chemically defined media, cell culture scientists screen many additives to improve cell growth and productivity. However, the introduction or increase of supplements, typically considered beneficial or pr