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An efficient method for purification of human T-cell growth factor.

Abstract:
A 1000-fold purification of human T-cell growth factor (TCGF) was achieved starting from supernatants of human spleen cells stimulated with phytohaemagglutinin (PHA) in culture medium containing 0.5% serum. The purification scheme involved precipitation with ammonium sulphate, gel filtration and blue-Sepharose chromatography. The use of polyethylene glycol 6000 (PEG 6000) was critical during the chromatographic steps in order to obtain high final recoveries or activity (40-50%). Purified preparations of TCGF labelled with 125I by the chloramine T method revealed that the activity co-migrated with 2 molecular species of 14,000-17,000 daltons in SDS-PAGE under non-reducing conditions.
Publication status:
Published

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Publisher copy:
10.1016/0022-1759(82)90236-8

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author


Journal:
Journal of immunological methods More from this journal
Volume:
53
Issue:
1
Pages:
15-26
Publication date:
1982-08-01
DOI:
EISSN:
1872-7905
ISSN:
0022-1759


Language:
English
Keywords:
Pubs id:
pubs:18617
UUID:
uuid:bb993a3a-c155-46cb-85a9-ed1c8715733a
Local pid:
pubs:18617
Source identifiers:
18617
Deposit date:
2012-12-19

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