A simple method for large‐scale purification of plasma‐derived apo‐transferrin

Abstract

We investigated and optimized a purification process, suitable for industrial scale, to obtain pharmaceutical grade apo-Tf (apo-transferrin), preserving its physiological properties and functions. Apo-Tf was obtained from fraction IV subfraction 1 and IV subfraction 4 (fraction IV-1,4), a waste product of the Cohn fractionation process, performing a single chromatographic run and two viral inactivation/removal steps. The structural integrity and the biological activity of the final product were extensively tested. The yield of apo-Tf produced was 80% on laboratory scale and 90% in scale-up lots, and the purity was higher than 95%. The purified protein preserves iron- and receptor-binding activities and shows a normal glycosylation pattern. The single chromatographic step process presented here provides an efficient means to prepare commercial quantities of the protein. The final product is sterile and two viral inactivation/removal steps were introduced into the process.

A novel formulation of theranostic nanomedicine for targeting drug delivery to gastrointestinal tract cancer

“…Transferrin receptors' expression has attracted researchers for targeting drug delivery on rapidly growing cells (Iinuma et al 2002). Transferrin is an important growth-promoting protein due to its iron-binding property (Ascione et al 2010) and its expression is elevated in cancer cells due to increased uptake of iron in cancer cells for high metabolic pathways (Daniels et al 2006b). Therefore, a positive correlation exists between cancer cells and transferrin receptor expression (Trowbridge and Omary 2006;Luria-Pérez et al 2016;Kwok 2002).…”

Engineering Quantum Dot (Cadmium Sulfide) on Antibodies for Fluoroimmunoassays

“…This relationship makes transferrin receptor an important target for targeting drug delivery by using either transferrin protein [25,26] or anti-transferrin receptor antibody [27]. Other than transferrin applications for targeting drug delivery, transferrin also has free-iron sequestering, antioxidative, and antimicrobial actions that enhance its importance in several therapeutic applications including reperfusion injury, ischemia, organ transplantation, and cardiovascular diseases [28][29][30][31].…”

Large‐scale purification of high purity α1‐antitrypsin from Cohn Fraction IV with virus inactivation by solvent/detergent and dry‐heat treatment

“…Better utilization of Cohn F IV is a main research interest in our laboratory, and several important proteins such as α2‐M and haptoglobin have been isolated with high purity in our laboratory. Other plasma‐derived proteins such vitamin D‐binding protein and apo‐Tf also have been isolated successfully from Cohn F IV. Cohn F IV is a desirable starting material for purification of plasma proteins, especially for proteins with low concentrations in plasma since purifying low concentration proteins directly from plasma is costly and unrealistic.…”