Improved purification of the human placental transferrin receptor and a novel immunoradiometric assay for receptor protein

Anderson G.J., Mackerras A., Powell L.W. and Halliday J.W. (1986) Improved purification of the human placental transferrin receptor and a novel immunoradiometric assay for receptor protein. BBA - General Subjects, 884 2: 225-233. doi:10.1016/0304-4165(86)90167-4


Author Anderson G.J.
Mackerras A.
Powell L.W.
Halliday J.W.
Title Improved purification of the human placental transferrin receptor and a novel immunoradiometric assay for receptor protein
Journal name BBA - General Subjects   Check publisher's open access policy
ISSN 0304-4165
Publication date 1986-11-19
Sub-type Article (original research)
DOI 10.1016/0304-4165(86)90167-4
Open Access Status Not yet assessed
Volume 884
Issue 2
Start page 225
End page 233
Total pages 9
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract A simplified method for the purification of human placental transferrin receptor is described. The procedure involves chromatography of a detergent extract of placenta on immobilized iron-loaded transferrin. Knowledge of the physiology of the interaction between transferrin and its receptor is applied to enable bound receptor to be eluted under mild conditions and essentially free of contaminating transferrin. Purified transferrin receptor and a monoclonal antibody to the receptor were used to developed a novel immunoradiometric assay for the receptor in which the monoclonal antibody is the radiolabelled species. A competition between two populations of receptor, one immobilized on a particulate support and the other in solution, provides the basis for the assay. Using this assay we have measured transferrin receptor levels in placental and hepatic tissue and in three cell lines during both the logarithmic and stationary phases of cell growth.
Keyword (Human placenta)
Immunoradiometric assay
Receptor purification
Transferrin receptor
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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