Abstract: The invention relates to a process for purifying a protein by mixing a protein preparation with a solution having a first salt and a second salt, wherein each salt has a different lyotropic value, and loading the mixture onto a hydrophobic interaction chromatography column. The dynamic capacity of the column for a protein using the two salt combination will be increased compared with the dynamic capacity of the column for either single salt alone.

Abstract: The invention relates to a process for purifying a protein by mixing a protein preparation with a solution having a first salt and a second salt, wherein each salt has a different lyotropic value, and loading the mixture onto a hydrophobic interaction chromatography column. The dynamic capacity of the column for a protein using the two salt combination will be increased compared with the dynamic capacity of the column for either single salt alone.

Abstract: The invention relates to a process for purifying a protein by mixing a protein preparation with a solution having a first salt and a second salt, wherein each salt has a different lyotropic value, and loading the mixture onto a hydrophobic interaction chromatography column. The dynamic capacity of the column for a protein using the two salt combination will be increased compared with the dynamic capacity of the column for either single salt alone.

Abstract: The invention relates to a process for purifying a protein by mixing a protein preparation with a solution having a first salt and a second salt, wherein each salt has a different lyotropic value, and loading the mixture onto a hydrophobic interaction chromatography column. The dynamic capacity of the column for a protein using the two salt combination will be increased compared with the the dynamic capacity of the column for either single salt alone.

Abstract: The present invention provides methods of stabilizing a protein at low pH by mixing the protein in a solution with one or more stabilizers in sufficient quantity to reduce the degree of aggregation of the protein at a low pH. In one embodiment, the stabilizers are selected from one or more of the following amino acids: glycine, leucine, lysine, alanine, methionine, aspartic acid and its salts, glutamic acid and its salts, arginine, tyrosine, and histidine. The methods of stabilizing a protein preparation find particular utility in stabilizing a protein during a low pH viral inactivation procedure.