Antibody purification from human plasma by metal-chelated affinity membranes

Handan Yavuz; Nilay Bereli; Fatma Yılmaz; Canan Armutcu; Adil Denizli

doi:10.1007/978-1-4939-2447-9_4

Antibody purification from human plasma by metal-chelated affinity membranes

Division of Biochemistry

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Immobilized metal ion affinity chromatography (IMAC) has been used for purification of proteins. IMAC introduces a new approach for selectively interacting biomolecules on the basis of their affinities for metal ions. The separation is based on different binding abilities of the proteins to the chelated metal ions on support. Here, N-methacryloyl-(L)-histidine methyl ester (MAH) is used as the metal-chelating ligand. Poly(hydroxyethyl methacrylate) Poly(HEMA) based membranes were prepared by photo-polymerization technique. Then, Zn²⁺, Ni²⁺, Co²⁺, and Cu²⁺ ions were chelated directly on the poly(HEMA-MAH) membranes for purification of immunoglobulin G (IgG) from human plasma.

Original language	English
Pages (from-to)	43-46
Number of pages	4
Journal	Methods in Molecular Biology
Volume	1286
DOIs	https://doi.org/10.1007/978-1-4939-2447-9_4
Publication status	Published - 2015

Keywords

Affinity membranes
Antibody purification
IMAC
Immunoglobulin-G
Poly(HEMA)

Access to Document

10.1007/978-1-4939-2447-9_4

Cite this

@article{a00e564b9dc84f9791c7992522f987ad,

title = "Antibody purification from human plasma by metal-chelated affinity membranes",

abstract = "Immobilized metal ion affinity chromatography (IMAC) has been used for purification of proteins. IMAC introduces a new approach for selectively interacting biomolecules on the basis of their affinities for metal ions. The separation is based on different binding abilities of the proteins to the chelated metal ions on support. Here, N-methacryloyl-(L)-histidine methyl ester (MAH) is used as the metal-chelating ligand. Poly(hydroxyethyl methacrylate) Poly(HEMA) based membranes were prepared by photo-polymerization technique. Then, Zn2+, Ni2+, Co2+, and Cu2+ ions were chelated directly on the poly(HEMA-MAH) membranes for purification of immunoglobulin G (IgG) from human plasma.",

keywords = "Affinity membranes, Antibody purification, IMAC, Immunoglobulin-G, Poly(HEMA)",

author = "Handan Yavuz and Nilay Bereli and Fatma Yılmaz and Canan Armutcu and Adil Denizli",

note = "Publisher Copyright: {\textcopyright} Springer Science+Business Media New York 2015.",

year = "2015",

doi = "10.1007/978-1-4939-2447-9\_4",

language = "English",

volume = "1286",

pages = "43--46",

journal = "Methods in Molecular Biology",

issn = "1064-3745",

publisher = "Humana Press Inc.",

}

TY - JOUR

T1 - Antibody purification from human plasma by metal-chelated affinity membranes

AU - Yavuz, Handan

AU - Bereli, Nilay

AU - Yılmaz, Fatma

AU - Armutcu, Canan

AU - Denizli, Adil

N1 - Publisher Copyright: © Springer Science+Business Media New York 2015.

PY - 2015

Y1 - 2015

N2 - Immobilized metal ion affinity chromatography (IMAC) has been used for purification of proteins. IMAC introduces a new approach for selectively interacting biomolecules on the basis of their affinities for metal ions. The separation is based on different binding abilities of the proteins to the chelated metal ions on support. Here, N-methacryloyl-(L)-histidine methyl ester (MAH) is used as the metal-chelating ligand. Poly(hydroxyethyl methacrylate) Poly(HEMA) based membranes were prepared by photo-polymerization technique. Then, Zn2+, Ni2+, Co2+, and Cu2+ ions were chelated directly on the poly(HEMA-MAH) membranes for purification of immunoglobulin G (IgG) from human plasma.

AB - Immobilized metal ion affinity chromatography (IMAC) has been used for purification of proteins. IMAC introduces a new approach for selectively interacting biomolecules on the basis of their affinities for metal ions. The separation is based on different binding abilities of the proteins to the chelated metal ions on support. Here, N-methacryloyl-(L)-histidine methyl ester (MAH) is used as the metal-chelating ligand. Poly(hydroxyethyl methacrylate) Poly(HEMA) based membranes were prepared by photo-polymerization technique. Then, Zn2+, Ni2+, Co2+, and Cu2+ ions were chelated directly on the poly(HEMA-MAH) membranes for purification of immunoglobulin G (IgG) from human plasma.

KW - Affinity membranes

KW - Antibody purification

KW - IMAC

KW - Immunoglobulin-G

KW - Poly(HEMA)

UR - https://www.scopus.com/pages/publications/84924368825

U2 - 10.1007/978-1-4939-2447-9_4

DO - 10.1007/978-1-4939-2447-9_4

M3 - Article

C2 - 25749944

AN - SCOPUS:84924368825

SN - 1064-3745

VL - 1286

SP - 43

EP - 46

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

ER -

Antibody purification from human plasma by metal-chelated affinity membranes

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this