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. 2023 Jun 13;13:9579. doi: 10.1038/s41598-023-36492-8

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Purification of bovine lactoferrin (bLF). (A) Typical elution profile of bLF on CM-Sephadex C50 column. The lactoferrin (●▬●) was eluted at a salt gradient of 0.2–0.6 M NaCl (▬). All eluted fractions were immunoassayed for bLF confirmation (▲▬▲), and bLF was eluted in the first and second peaks. (B) 12% SDS-PAGE for bLF during purification steps. Lane 1 is protein marker, lane 2 is the raw bovine whey, lane 3 is bLF eluted from CM Sephadex C50 column and lane 4 is purified bLF eluted from Sephacryl S200 column.