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. 2017 Jun 8;7:3053. doi: 10.1038/s41598-017-03285-9

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© The Author(s) 2017

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Purification and characterization of recombinant human PLTP from PLTPTg rabbit milk. (A) After FPLC elution of clarified milk proteins on a Heparin Sepharose 6 Fast Flow column, using a discontinuous NaCl gradient with 100 mM step increases, different fractions (A–G) were collected at different NaCl concentrations and analyzed for specific PLTP activity. The fraction exhibiting the highest specific PLTP activity (G) was eluted at the 300 mM NaCl step. (B and C) Electrophoretic analysis of purified rhPLTP (B) shows a sharp, 60 kDa band which was analyzed by MALDI-TOF/TOF MS and a database search. The protein (arrow) was identified as human PLTP according to the matched peptides which are shown in bold red (C). (MW: 54.7 kDa. Number of matching peptides: 24. Sequence coverage: 39.8%. Score: 182 for a significant matching score above 50). (D) Comparison of the phospholipid transfer activities of active purified rhPLTP, wild-type (WT) mouse plasma, Pltp−/− mouse plasma, and PBS buffer. The active rhPLTP shows phospholipid transfer activity of the same magnitude as that in WT mouse plasma.