Corrections to Purification Tools for Monoclonal Antibodies
You might think that after working on a book for a solid year, that there couldn't possibly be any mistakes left. Well, not many at least, but some got through. We apologize for any confusion they cause and list corrections on this page. If you encounter errors we haven't listed, please notify us and we'll post the corrections here. Thanks for your understanding.
Page 11: Table 2.2 , the third column of numbers, from top to bottom, instead of all being 65%, should be as follows: 65%, 59%, 72%, 63%, 58%, 60%, 61%, 74%, 69%, 62%
Page 67: Figure 4.7 depicts anion exchange profiles
Page 87 - 102: Chapter 5. Hydroxyapatite Chromatography. This isn't a correction per se, but just a note that a great deal has been learned about antibody puriification with hydroxyapatite since publication. Some of this information is contained in a web article entitled "An Enigma Unmasked: How Hydroxyapatite Works and How to Make it Work for You." You can download a copy from our downstream processing library, as well as number of more recent oral presentations and posters.
Page 105: The correct Figure number is 6.2
Page 128: At the end of paragraph 2, it says that selectivity is otherwise relatively salt independent, even up to concentrations of 5.0M sodium chloride. This is true to the extent that binding of IgG is not attenuated by elevated concentrations of sodium chloride, or sodium sulfate. However, the higher the salt concentration, the higher the binding of non-IgG contaminants. This is especially true with precipitating salts like sodium sulfate. Purification performance can suffer significantly. If it's necessary or desirable to load an IMAC column in high salt, you can switch to a low-salt buffer before you elute. This will "elute" most of the nonspecific contaminants. Another caution; we've found that IgG binding on Ni-IDA columns is attenuated by high phosphate concentrations.
Page 161: Table 9.1, legend, line 4: "HM" should be "MG".
Page 222: The binding buffer for mouse IgG includes 1.0M sodium sulfate. Depending on the protein-A media you use, this may be too high, in which case you'll observe a lot of nonspecific contaminant binding. If you encounter this problem, back off the sodium sulfate concentration to ~0.75M, lower if necessary. Better still, use a substitute sodium chloride. It requires a higher molar concentration but you won't get the nonspecific binding.
Page 251: "Plese" should, of course, be spelled "Please".
Validated Biosystems Resource Guide for Downstream Processing
is a service of Validated Biosystems Inc.
©1996–2006 Validated Biosystems Inc. All rights reserved