Abstract |
Eighty-nine human breast tumor progesterone receptors were assayed both by a radioligand assay (RLA; 3H- ORG-2058) and by the enzyme immunoassay from Abbott Laboratories (PR-EIA). The correlation obtained between the two methods was EIA = 0.83 RLA + 4.1 fmol/mg protein (r = 0.83). Great discrepancies were observed with EIA/RLA ratios varying from 0.5 to 2. After KCl 0.4 mol/l dissociation and chromatographic separation of 8 PR isoforms [12], the two PR polymeric forms ( isoforms 1 and 2) which remained bound to the hsp90 heat shock protein were not or only partially detected by EIA, whereas PR-hsp70 isoforms were highly detected with EIA/RLA ratios increased up to 3.8. Free PR-A and PR-B proteins and the PR-truncated form (52 kDa) were never detected by EIA. Thus, the final result of PR assay using the Abbott method depends directly on the amount of PR-hsp70 isoforms produced through KCl dissociation during the overnight incubation of PR with the KD68 coated beads.
|
Authors | J Goussard, E Lemoisson, H Cren |
Journal | Annales de biologie clinique
(Ann Biol Clin (Paris))
Vol. 53
Issue 3
Pg. 107-13
( 1995)
ISSN: 0003-3898 [Print] France |
PMID | 7574094
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
|
Chemical References |
- Epitopes
- HSP70 Heat-Shock Proteins
- HSP90 Heat-Shock Proteins
- Isoenzymes
- Receptors, Progesterone
|
Topics |
- Breast Neoplasms
(metabolism)
- Epitopes
(metabolism)
- Female
- HSP70 Heat-Shock Proteins
(metabolism)
- HSP90 Heat-Shock Proteins
(metabolism)
- Humans
- Immunoenzyme Techniques
- Isoenzymes
(analysis)
- Radioligand Assay
- Receptors, Progesterone
(analysis, chemistry, immunology)
|