Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech Solution

A fast and simple biotech method is presented for the simultaneous isolation and purification of transferrin (Tf) and immunoglobulin G (IgG) from the same pool-sample of human serum, yielding >98% pure proteins. Serum sample preparation was achieved by precipitation with ethacridine lactate (riva...

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Main Authors: Danilo Četić, Goran Miljuš, Zorana Dobrijević, Nikola Gligorijević, Aleksandra Vilotić, Olgica Nedić, Ana Penezić
Format: Article
Language:English
Published: MDPI AG 2025-02-01
Series:Molecules
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Online Access:https://www.mdpi.com/1420-3049/30/5/993
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author Danilo Četić
Goran Miljuš
Zorana Dobrijević
Nikola Gligorijević
Aleksandra Vilotić
Olgica Nedić
Ana Penezić
author_facet Danilo Četić
Goran Miljuš
Zorana Dobrijević
Nikola Gligorijević
Aleksandra Vilotić
Olgica Nedić
Ana Penezić
author_sort Danilo Četić
collection DOAJ
description A fast and simple biotech method is presented for the simultaneous isolation and purification of transferrin (Tf) and immunoglobulin G (IgG) from the same pool-sample of human serum, yielding >98% pure proteins. Serum sample preparation was achieved by precipitation with ethacridine lactate (rivanol). Protein purification was performed with AKTA Avant 150 FPLC, using a Resource Q column. Three different buffers at pH 6.2 (MES, phosphate, and Bis-Tris) were tested. Isolated and purified proteins retained their native 3D structure, as shown by spectrofluorimetric measurements. Tf functionality was preserved, as confirmed by the retention of both the iron binding capacity and its ability to interact with the transferrin receptor (immunofluorescent staining), as well as the immunogenicity of IgG, as shown by Western blot analysis with immunodetection. The formation of IgG aggregates was avoided. This biotech method is a rapid, simple, and time-saving alternative to other methods for the isolation of extremely pure IgG and Tf, while it is also the only method so far described for their simultaneous isolation.
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spelling doaj-art-714c151ce1c24829b429f09b695331ac2025-08-20T02:53:22ZengMDPI AGMolecules1420-30492025-02-0130599310.3390/molecules30050993Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech SolutionDanilo Četić0Goran Miljuš1Zorana Dobrijević2Nikola Gligorijević3Aleksandra Vilotić4Olgica Nedić5Ana Penezić6Institute for the Application of Nuclear Energy INEP, University of Belgrade, Banatska 31 b, 11000 Belgrade, SerbiaInstitute for the Application of Nuclear Energy INEP, University of Belgrade, Banatska 31 b, 11000 Belgrade, SerbiaInstitute for the Application of Nuclear Energy INEP, University of Belgrade, Banatska 31 b, 11000 Belgrade, SerbiaInstitute for the Application of Nuclear Energy INEP, University of Belgrade, Banatska 31 b, 11000 Belgrade, SerbiaInstitute for the Application of Nuclear Energy INEP, University of Belgrade, Banatska 31 b, 11000 Belgrade, SerbiaInstitute for the Application of Nuclear Energy INEP, University of Belgrade, Banatska 31 b, 11000 Belgrade, SerbiaInstitute for the Application of Nuclear Energy INEP, University of Belgrade, Banatska 31 b, 11000 Belgrade, SerbiaA fast and simple biotech method is presented for the simultaneous isolation and purification of transferrin (Tf) and immunoglobulin G (IgG) from the same pool-sample of human serum, yielding >98% pure proteins. Serum sample preparation was achieved by precipitation with ethacridine lactate (rivanol). Protein purification was performed with AKTA Avant 150 FPLC, using a Resource Q column. Three different buffers at pH 6.2 (MES, phosphate, and Bis-Tris) were tested. Isolated and purified proteins retained their native 3D structure, as shown by spectrofluorimetric measurements. Tf functionality was preserved, as confirmed by the retention of both the iron binding capacity and its ability to interact with the transferrin receptor (immunofluorescent staining), as well as the immunogenicity of IgG, as shown by Western blot analysis with immunodetection. The formation of IgG aggregates was avoided. This biotech method is a rapid, simple, and time-saving alternative to other methods for the isolation of extremely pure IgG and Tf, while it is also the only method so far described for their simultaneous isolation.https://www.mdpi.com/1420-3049/30/5/993biotherapeuticsisolation and purificationion-exchangeIgGtransferrin
spellingShingle Danilo Četić
Goran Miljuš
Zorana Dobrijević
Nikola Gligorijević
Aleksandra Vilotić
Olgica Nedić
Ana Penezić
Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech Solution
Molecules
biotherapeutics
isolation and purification
ion-exchange
IgG
transferrin
title Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech Solution
title_full Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech Solution
title_fullStr Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech Solution
title_full_unstemmed Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech Solution
title_short Simultaneous Isolation and Purification of Transferrin and Immunoglobulin G from Human Serum—A New Biotech Solution
title_sort simultaneous isolation and purification of transferrin and immunoglobulin g from human serum a new biotech solution
topic biotherapeutics
isolation and purification
ion-exchange
IgG
transferrin
url https://www.mdpi.com/1420-3049/30/5/993
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