Fab fragment immobilized immunoaffinity cryogels as a tool for human serum albumin purification: Characterization of Fab immobilized cryogels.

Authors

Sabina Huseynli, Duygu Çimen, Nilay Bereli̇, A. Deni̇zli̇

Published

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 2022

DOI

10.1016/j.jchromb.2022.123311

Citations

7

Abstract

As a general approach Fab immobilized immunoaffinity cryogels for human serum albumin purification is presented in this article. The directed immobilization of antibodies, which have been used as diagnostic and therapeutic agents in applications recently, has brought a different perspective to the purification method. In our study to shed light on this method, anti-HSA Fab fragment immobilized poly(hydroxylethyl methacrylate-N-methacryloyl-(l)-cysteine) (PHEMAC-Fab) and PHEMAC cryogels were prepared for the purification of human serum albumin (HSA). The specific surface areas of the PHEMAC-Fab and PHEMAC cryogels were calculated as 38.6 m2/g, and 20.0 m2/g, respectively. In comparison, the maximum swelling ratio was observed in the PHEMAC-Fab cryogel and more water was absorbed than the PHEMAC cryogel. While the macropore ratio in the PHEMAC-Fab cryogel is 54.3%, the macropore ratio of the PHEMAC cryogels is 41.6%. The results obtained here showed that anti-HSA cryogel prepared by immobilization of Fab fragments can be an alternative to traditional immunoaffinity techniques for HSA purification.

Cite this article

BibTeX

@article{sabina2022,
  title   = {Fab fragment immobilized immunoaffinity cryogels as a tool for human serum albumin purification: Characterization of Fab immobilized cryogels.},
  author  = {Sabina Huseynli and Duygu Çimen and Nilay Bereli̇ and A. Deni̇zli̇},
  journal = {Journal of chromatography. B, Analytical technologies in the biomedical and life sciences},
  doi     = {10.1016/j.jchromb.2022.123311},
  year    = {2022}
}

← All publications DOI: 10.1016/j.jchromb.2022.123311