Purification of rabbit polyclonal immunoglobulin G using anion exchangers.

Negative chromatography antibody purification (N-CAP) using the weak anion exchanger STREAMLINE™ DEAE to extract impurities while retaining the target antibody is proposed as an effective method for the recovery of antibody from rabbit serum. The effects of pH and initial protein concentration on th...

Full description

Saved in:
Bibliographic Details
Main Authors: Tey, Beng Ti, Taip, Farah Saleena, Tan, Wen Siang, Ling, Tau Chuan, Wongchuphan, Rattana, Subramaniam, Senthil Kumar
Format: Article
Language:English
English
Published: 2011
Online Access:http://psasir.upm.edu.my/id/eprint/23385/1/Purification%20of%20rabbit%20polyclonal%20immunoglobulin%20G%20using%20anion%20exchangers.pdf
http://psasir.upm.edu.my/id/eprint/23385/
Tags: Add Tag
No Tags, Be the first to tag this record!
id my.upm.eprints.23385
record_format eprints
spelling my.upm.eprints.233852016-01-12T04:47:51Z http://psasir.upm.edu.my/id/eprint/23385/ Purification of rabbit polyclonal immunoglobulin G using anion exchangers. Tey, Beng Ti Taip, Farah Saleena Tan, Wen Siang Ling, Tau Chuan Wongchuphan, Rattana Subramaniam, Senthil Kumar Negative chromatography antibody purification (N-CAP) using the weak anion exchanger STREAMLINE™ DEAE to extract impurities while retaining the target antibody is proposed as an effective method for the recovery of antibody from rabbit serum. The effects of pH and initial protein concentration on the removal of albumin were investigated. The optimal pH and initial protein concentration for the efficient removal of albumin from rabbit serum were pH 8.0 and 0.5 mg/ml, respectively. Under optimal binding conditions, DEAE successfully removed more than 90% of the albumin from rabbit serum with less than 20% IgG loss. This process offered good polyclonal IgG yield of 80% with a purity of 83% and a purification factor of 5.5. The use of a strong anion exchanger like STREAMLINE™ Q XL for albumin removal was also explored. Under similar optimized conditions, albumin removal by Q XL was as high as 90%. However, IgG recovery and purity were reduced to about 70% and 62%, respectively. Thus, N-CAP using the anion exchanger DEAE removes albumin from rabbit serum and thereby offers an efficient means of purifying polyclonal antibodies. 2011 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/23385/1/Purification%20of%20rabbit%20polyclonal%20immunoglobulin%20G%20using%20anion%20exchangers.pdf Tey, Beng Ti and Taip, Farah Saleena and Tan, Wen Siang and Ling, Tau Chuan and Wongchuphan, Rattana and Subramaniam, Senthil Kumar (2011) Purification of rabbit polyclonal immunoglobulin G using anion exchangers. Process Biochemistry, 46 (Januar). pp. 101-107. ISSN 1359-5113 10.1016/j.procbio.2010.07.023 English
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
English
description Negative chromatography antibody purification (N-CAP) using the weak anion exchanger STREAMLINE™ DEAE to extract impurities while retaining the target antibody is proposed as an effective method for the recovery of antibody from rabbit serum. The effects of pH and initial protein concentration on the removal of albumin were investigated. The optimal pH and initial protein concentration for the efficient removal of albumin from rabbit serum were pH 8.0 and 0.5 mg/ml, respectively. Under optimal binding conditions, DEAE successfully removed more than 90% of the albumin from rabbit serum with less than 20% IgG loss. This process offered good polyclonal IgG yield of 80% with a purity of 83% and a purification factor of 5.5. The use of a strong anion exchanger like STREAMLINE™ Q XL for albumin removal was also explored. Under similar optimized conditions, albumin removal by Q XL was as high as 90%. However, IgG recovery and purity were reduced to about 70% and 62%, respectively. Thus, N-CAP using the anion exchanger DEAE removes albumin from rabbit serum and thereby offers an efficient means of purifying polyclonal antibodies.
format Article
author Tey, Beng Ti
Taip, Farah Saleena
Tan, Wen Siang
Ling, Tau Chuan
Wongchuphan, Rattana
Subramaniam, Senthil Kumar
spellingShingle Tey, Beng Ti
Taip, Farah Saleena
Tan, Wen Siang
Ling, Tau Chuan
Wongchuphan, Rattana
Subramaniam, Senthil Kumar
Purification of rabbit polyclonal immunoglobulin G using anion exchangers.
author_facet Tey, Beng Ti
Taip, Farah Saleena
Tan, Wen Siang
Ling, Tau Chuan
Wongchuphan, Rattana
Subramaniam, Senthil Kumar
author_sort Tey, Beng Ti
title Purification of rabbit polyclonal immunoglobulin G using anion exchangers.
title_short Purification of rabbit polyclonal immunoglobulin G using anion exchangers.
title_full Purification of rabbit polyclonal immunoglobulin G using anion exchangers.
title_fullStr Purification of rabbit polyclonal immunoglobulin G using anion exchangers.
title_full_unstemmed Purification of rabbit polyclonal immunoglobulin G using anion exchangers.
title_sort purification of rabbit polyclonal immunoglobulin g using anion exchangers.
publishDate 2011
url http://psasir.upm.edu.my/id/eprint/23385/1/Purification%20of%20rabbit%20polyclonal%20immunoglobulin%20G%20using%20anion%20exchangers.pdf
http://psasir.upm.edu.my/id/eprint/23385/
_version_ 1643828042434347008
score 13.211869