Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Mahlet A. Woldeyes"'
Autor:
Amjad A. Chowdhury, Neha Manohar, Marta A. Witek, Mahlet A. Woldeyes, Ranajoy Majumdar, Ken K. Qian, William D. Kimball, Shifeng Xu, Alfredo Lanzaro, Thomas M. Truskett, Keith P. Johnston
Publikováno v:
Molecular Pharmaceutics.
Publikováno v:
Pharmaceutical research. 38(11)
Protein solubility is an important attribute of pharmaceutical monoclonal antibody (MAb) formulations, particularly at high MAb concentrations. PEG-induced protein precipitation has been routinely used to assess protein solubility. To provide insight
Publikováno v:
Molecular pharmaceutics. 17(12)
Protein solution viscosity (η) as a function of temperature was measured at a series of protein concentrations under a range of formulation conditions for two monoclonal antibodies (MAbs) and a globular protein (aCgn). Based on theoretical arguments
Autor:
Danielle L. Leiske, Eric M. Furst, Christopher J. Roberts, William J. Galush, Mahlet A. Woldeyes, Lilian Lam Josephson
Publikováno v:
Molecular Pharmaceutics. 15:4745-4755
Solution viscosities (η) and protein-protein interactions (PPI) of three monoclonal antibodies (mAb-A, mAb-B, mAb-C), two bispecific antibodies (BsAb-A/B, BsAb-A/C), and two 1:1 binary mixtures (mAb-A + mAb-B and mAb-A + mAb-C) were measured. mAb-A
Publikováno v:
The Journal of Physical Chemistry B. 121:4756-4767
Protein interactions of α-chymotrypsinogen A (aCgn) were quantified using light scattering from low to high protein concentrations. Static light scattering (SLS) was used to determine the excess Rayleigh ratio (Rex) and osmotic second virial coeffic
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2039
Static and dynamic (laser) light scattering (SLS and DLS, respectively) can be used to measure the so-called weak or colloidal protein-protein interactions in solution from low to high protein concentrations (c
Publikováno v:
Methods in Molecular Biology ISBN: 9781493996773
Static and dynamic (laser) light scattering (SLS and DLS, respectively) can be used to measure the so-called weak or colloidal protein-protein interactions in solution from low to high protein concentrations (c2). This chapter describes a methodology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c6d39cdb6183779a4f0e3e532710c684
https://doi.org/10.1007/978-1-4939-9678-0_2
https://doi.org/10.1007/978-1-4939-9678-0_2
Autor:
Bernhardt L. Trout, Kristen E. Whaley, Ying Diao, Mahlet A. Woldeyes, T. Alan Hatton, Patrick S. Doyle, Matthew E. Helgeson, Allan S. Myerson
Publikováno v:
Journal of the American Chemical Society. 134:673-684
Although nanoporous materials have been explored for controlling crystallization of polymorphs in recent years, polymorphism in confined environments is still poorly understood, particularly from a kinetic perspective, and the role of the local struc