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Theodore W. Randolph

Researcher at University of Colorado Boulder

Publications -  313
Citations -  22031

Theodore W. Randolph is an academic researcher from University of Colorado Boulder. The author has contributed to research in topics: Protein aggregation & Supercritical fluid. The author has an hindex of 77, co-authored 306 publications receiving 20474 citations. Previous affiliations of Theodore W. Randolph include MedImmune & University of Colorado Denver.

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Effects of Additives on the Stability of Humicola Lanuginosa Lipase During Freeze-Drying and Storage in the Dried Solid

TL;DR: The effects of various classes of additives on the stability of a protein with a relatively hydrophobic surface, Humicola lanuginosa lipase, during lyophilization and storage in the dried solid were investigated.
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Process variable implications for residual solvent removal and polymer morphology in the formation of gentamycin-loaded poly (L-lactide) microparticles.

TL;DR: XRD and DSC analysis on these samples suggest that those produced at lower CO2co-flow rates have a higher degree of crystallinity, which increases the diffusivity of DCM through the polymer matrix, which determines the solvent removal rates.
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Effects of Sugars and Polymers on Crystallization of Poly(ethylene glycol) in Frozen Solutions: Phase Separation Between Incompatible Polymers

TL;DR: This study examined the effect of third components (low-molecular-weight saccharides and polymers) on the crystallization of poly(ethylene) glycol (PEG) in frozen solutions, focusing on the relationship between their crystallization-inhibiting ability and molecular compatibility.
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High Concentration Formulations of Recombinant Human Interleukin-1 Receptor Antagonist: II. Aggregation Kinetics

TL;DR: Increasing the protein concentration to 100 mg/mL shifts the rhIL-1ra monomer-dimer equilibrium significantly at low ionic strength to favor dimerization, which is reflected in subtle conformational changes in the circular dichroism and second-derivative FTIR spectra.
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IgG1 Aggregation and Particle Formation Induced by Silicone–water Interfaces on Siliconized Borosilicate Glass Beads: A Model for Siliconized Primary Containers

TL;DR: Agitation of protein formulations in the presence of siliconized glass beads provides a model for baked-on silicone oil-water interface in prefilled syringes and a means by which to evaluate particle formation and aggregation during formulation screening.