PMID- 6203983
OWN - NLM
STAT- MEDLINE
DCOM- 19840820
LR  - 20181130
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 133
IP  - 2
DP  - 1984 Aug
TI  - The behavior of the solubilized receptor for immunoglobulin E in polyethylene 
      glycol-detergent solutions: characterization and potential applications.
PG  - 863-71
AB  - We studied the effect of polyethylene glycol (PEG) on the solubility of the 
      receptor for immunoglobulin E (IgE) in non-ionic detergent extracts of rat 
      basophilic leukemia (RBL) cells. We found that the precipitation patterns of free 
      and IgE-bound receptor were identical but differed from that of unbound IgE. 
      Thus, 85 to 95% of the free receptor and the IgE-receptor complexes precipitated 
      at 13% PEG in the presence of 0.5% Nonidet P-40, whereas 95% of the unbound IgE 
      remained soluble. A similar degree of differentiation between the precipitation 
      of receptor-bound and unbound IgE was found when we used extracts and PEG 
      solutions prepared with several non-ionic and/or neutral detergents. The intact 
      IgE-receptor complex with the full complement of subunits (alpha, beta, gamma) 
      precipitated more efficiently than the IgE-alpha-chain-complex. The presence of 
      phospholipids, which were previously shown to be important for preservation of 
      the association between the receptor subunits, enhanced the efficiency of 
      precipitation of the IgE-receptor complex. The presence of PEG also had an effect 
      on the solubility of cellular phospholipids and some of the detergents, although 
      the effect of PEG on either could not be directly related to its effect on the 
      solubility of the IgE-receptor complex. The radioiodinated receptor for IgE, much 
      like other radioiodinated RBL cell membrane proteins, was soluble (greater than 
      or equal to 95%) at approximately 7% PEG but could be specifically and 
      efficiently precipitated from crude cell extracts, in the presence of 7% PEG upon 
      the addition of anti-receptor immunoglobulins alone. Using mouse 
      anti-dinitrophenyl IgE antibody, we found that unlike unbound antigen (DNP-BGG) 
      or the IgE-receptor complex, the detergent-solubilized DNP-BGG-IgE-receptor 
      complex was insoluble at 7% PEG. Consequently, PEG can be employed in assays to 
      quantitate the soluble receptor, and to immunoprecipitate it specifically and 
      directly. Moreover, the use of PEG can facilitate the distinction between unbound 
      antigen and antigen-IgE-receptor complex as well as between the latter and 
      IgE-receptor complex.
FAU - Rivera, J
AU  - Rivera J
FAU - Rivnay, B
AU  - Rivnay B
FAU - Furuichi, K
AU  - Furuichi K
FAU - Isersky, C
AU  - Isersky C
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Detergents)
RN  - 0 (Membrane Proteins)
RN  - 0 (Receptors, IgE)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Solutions)
RN  - 0 (Surface-Active Agents)
RN  - 0 (dinitrophenyl gamma globulin)
RN  - 0 (gamma-Globulins)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - 3WJQ0SDW1A (Polyethylene Glycols)
SB  - IM
MH  - Animals
MH  - Basophils/metabolism
MH  - Chemical Precipitation
MH  - Detergents/*pharmacology
MH  - Immunoglobulin E/*metabolism
MH  - Leukemia, Experimental/immunology/metabolism
MH  - Membrane Proteins/metabolism
MH  - Polyethylene Glycols/*pharmacology
MH  - Rats
MH  - Receptors, IgE
MH  - Receptors, Immunologic/analysis/drug effects/*metabolism
MH  - Solubility
MH  - Solutions
MH  - Surface-Active Agents/*pharmacology
MH  - gamma-Globulins/analysis
EDAT- 1984/08/01 00:00
MHDA- 1984/08/01 00:01
CRDT- 1984/08/01 00:00
PHST- 1984/08/01 00:00 [pubmed]
PHST- 1984/08/01 00:01 [medline]
PHST- 1984/08/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1984 Aug;133(2):863-71.