Small molecule clearance in ultrafiltration/diafiltration in relation to protein interactions: Study of citrate binding to a fab

C. Harinarayan, K. Skidmore, Y. Kao, Andrew Zydney, R. Van Reis

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Ultrafiltration/diafiltration (UFDF) is commonly utilized in the purification of recombinant proteins to concentrate and buffer exchange the product. It is often the final step in the purification process, placing the protein in its final formulation and clearing small molecules introduced in upstream purification steps. This article presents a case study of reduced small molecule clearance in ultrafiltration/diafiltration of an antigen-binding fragment of a monoclonal antibody. Citrate, a commonly utilized small molecule in downstream processes, is shown to have reduced clearance due to specific interactions with the protein product. The study presents process solutions and utilizes a simple model to characterize clearance of small molecules which exhibit interactions with product protein.

Original languageEnglish (US)
Pages (from-to)1718-1722
Number of pages5
JournalBiotechnology and bioengineering
Volume102
Issue number6
DOIs
StatePublished - Apr 15 2009

Fingerprint

Ultrafiltration
Citric Acid
Purification
Proteins
Molecules
Recombinant Proteins
Recombinant proteins
Monoclonal antibodies
Buffers
Antigens
Monoclonal Antibodies
Ion exchange

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

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Small molecule clearance in ultrafiltration/diafiltration in relation to protein interactions : Study of citrate binding to a fab. / Harinarayan, C.; Skidmore, K.; Kao, Y.; Zydney, Andrew; Van Reis, R.

In: Biotechnology and bioengineering, Vol. 102, No. 6, 15.04.2009, p. 1718-1722.

Research output: Contribution to journalArticle

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AU - Van Reis, R.

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