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John Tharakan

Researcher at Howard University

Publications -  36
Citations -  670

John Tharakan is an academic researcher from Howard University. The author has contributed to research in topics: Engineering education & Cell culture. The author has an hindex of 16, co-authored 31 publications receiving 655 citations. Previous affiliations of John Tharakan include American Red Cross & University of California, San Diego.

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Serum‐free media in hybridoma culture and monoclonal antibody production

TL;DR: In general, serum‐free media which are “lipid rich” can sustain cell growth rates approaching that of serum supplemented cultures, however, specific antibody secretion rate is usually higher in serum‐ free media, irrespective of the lipid content.
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A radial flow hollow fiber bioreactor for the large‐scale culture of mammalian cells

TL;DR: A radial flow hollow fiber bioreactor has been developed that maximizes the utilization of fiber surface for cell growth while eliminating nutrient and metabolic gradients inherent in conventional hollow fiber cartridges.
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Operation and pressure distribution of immobilized cell hollow fiber bioreactors

TL;DR: Pressure‐drop data on hollow fiber cartridges which are in flow configurations typical of immobilized cell culture work is provided to illuminate operational problems that may arise in the culture of either anchorage dependent or independent cells.
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Physical and biochemical characterization of five commercial resins for immunoaffinity purification of factor IX.

TL;DR: The results demonstrate a straightforward method of assessing the feasibility of using particular resins in large-scale affinity purification of FIX, and the physical and biochemical properties studied included the crushability and ability to support increasing flow-rates at increasing pressures.
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Development of an immunoaffinity process for factor IX purification.

TL;DR: The use of solvent/detergent treatment as a potential viral inactivation method is incorporated in the process and shows no detectable leakage of monoclonal antibodies (MAb), efficient utilization of MAb, and provides yields greater than 95%.