1996
DOI: 10.1038/nbt0596-651
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Improved removal of viruslike particles from purified monoclonal antibody IgM preparation via virus filtration

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Cited by 8 publications
(2 citation statements)
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“…Realistically, viruses the size of polio-or parvoviruses (20-25 nm) cannot be separated from similarly sized proteins by such filters, since in this size range larger proteins are already held back. Yet Maerz et al 1 Success in solving this separation problem may be attributed to the different static properties of viruses and antibodies. Antibodies are very flexible and can slip through the narrow membrane pores at slow flow rates, whereas small, nonenveloped viruses must be considered to be rigid molecules that are restrained by the membrane.…”
Section: Viral Clearancementioning
confidence: 99%
“…Realistically, viruses the size of polio-or parvoviruses (20-25 nm) cannot be separated from similarly sized proteins by such filters, since in this size range larger proteins are already held back. Yet Maerz et al 1 Success in solving this separation problem may be attributed to the different static properties of viruses and antibodies. Antibodies are very flexible and can slip through the narrow membrane pores at slow flow rates, whereas small, nonenveloped viruses must be considered to be rigid molecules that are restrained by the membrane.…”
Section: Viral Clearancementioning
confidence: 99%
“…Recently, large pore ultrafiltration membranes with MWCO (150$800 kDa) have been developed as virus filtration membranes (Christy and Vermant, 2002;Hamamoto et al, 1989;Maerz et al, 1996). Here the aim is to validate virus clearance by greatly reducing the number of contaminating viruses by retaining virions that may be present in the product stream.…”
Section: Introductionmentioning
confidence: 99%