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Protein Expression Methods
Published in Jay L. Nadeau, Introduction to Experimental Biophysics, 2017
Most protein purification schemes begin with an affinity chromatography step. In affinity chromatography, the protein is specifically bonded to the column due to a characteristic of the protein and then eluted from the column in a competition experiment. A classic example of affinity chromatography is the purification of the nicotinic acetylcholine receptor from Torpedo electroplax. In this purification, the receptor’s affinity for α-bungarotoxin, a competitive antagonist, is used for protein purification by immobilizing α-bungarotoxin on a column and then passing the crude protein mixture over the column. In this process, only the nicotinic acetylcholine receptors stick to the column, and the nonspecific bond proteins can be eluted. The nicotinic acetylcholine receptor can subsequently be eluted from the column by addition of free α-bungarotoxin or another competitive agonist or antagonist of the receptor. While this is an extremely effective method for the purification of nicotinic acetylcholine receptors, it is not general and cannot be applied to all proteins.
Factors affecting therapeutic protein purity and yield during chromatographic purification
Published in Preparative Biochemistry & Biotechnology, 2023
Che Haznie Ayu Che Hussian, Wai Yie Leong
The pH-dependent nature of protein purification can greatly affect recovery yield and purity. It has been shown how phosphate buffers with pH ranges of 6.5–9 affect the recovery yield and purity of rhAT. Using mobile phase pH values of 6.5, 7, 7.5, 8, 8.5, and 9, the recovery yields (48, 50, 51, 53, 55, and 52%) and purities (97, 97, 98, 98, and 98%) were calculated experimentally. The best rhAT recovery yield (55%), as well as the highest purity (98%), have been demonstrated using a buffer with a pH of 8.5. The buffer with the lowest recovery yield (48%) and purity (97%) was pH 6.5. At pH 7.5, 8, and 9, recovery yields were poor (51%, 53%, and 52%) despite excellent purity (98%) as compared to pH 8.5. In a recent study, the impact of mobile phase pH on the purification of recombinant proteins was also successfully investigated.[86]
Resource allocation strategies for protein purification operations
Published in IISE Transactions, 2020
Yasemin Limon, Ananth Krishnamurthy
In this article, we investigate resource allocation issues in the context of protein purification projects. Protein purification is comprised of a series of steps that remove unwanted molecules from the protein manufactured during upstream fermentation operations. If the purification outcome does not satisfy the requirements in the first purification trial, it may be repeated by the same scientist or another scientist with different skills. The biomanufacturer incurs different costs depending upon the outcome obtained (success, repeat, or failure) and resource used (high skill or low skill). In addition to the risk of incurring higher costs, resource allocation decisions may cause delays in project timelines and loss of customer satisfaction.