PMID- 23928186
OWN - NLM
STAT- MEDLINE
DCOM- 20140714
LR  - 20220311
IS  - 1879-0542 (Electronic)
IS  - 0165-2478 (Linking)
VI  - 154
IP  - 1-2
DP  - 2013 Jul-Aug
TI  - Comparison of ELISA measurements of anti-Abeta concentrations and percentages of 
      specific binding to Abeta between unfractionated intravenous immunoglobulin products 
      and their purified anti-Abeta antibodies.
PG  - 7-11
LID - S0165-2478(13)00100-4 [pii]
LID - 10.1016/j.imlet.2013.07.008 [doi]
AB  - Intravenous immunoglobulin (IVIG) products are being investigated as possible 
      therapeutic agents for mild cognitive impairment and Alzheimer's disease (AD). 
      Anti-Abeta antibodies have been measured by ELISA in unfractionated IVIG products 
      and in affinity-purified antibodies from these products, but it is unclear if 
      similar results are obtained with these two approaches. Measurements of anti-Abeta 
      antibodies in unfractionated IVIG may be confounded by the presence of polyvalent 
      antibodies which can bind to multiple antigens, including those on ELISA plates; 
      whether this is an issue when measuring anti-Abeta antibodies in purified antibody 
      eluates from IVIG is also unknown. The objective of this study was to clarify 
      these issues. The concentrations of specific antibodies to Abeta1-42 monomer and the 
      percentages of specific binding to it were compared via ELISA between three 
      unfractionated IVIG products (Gamunex [Talecris], Gammagard [Baxter], and 
      Flebogamma [Grifols]) and their affinity-purified anti-Abeta antibodies. The 
      concentrations of anti-Abeta antibodies in unfractionated IVIG products were higher 
      than in their respective purified anti-Abeta eluates, and the rank order of the IVIG 
      products with respect to their anti-Abeta concentrations differed between the two 
      types of samples. The percentages of specific binding to Abeta were lower for 
      unfractionated IVIG than for purified anti-Abeta eluates. These findings indicate 
      that ELISA measurements of specific anti-Abeta antibodies and percentages of 
      specific binding to Abeta produce different results depending upon whether these 
      measurements are made in unfractionated IVIG products or their purified anti-Abeta 
      antibodies. Polyvalent binding occurs even with purified anti-Abeta antibodies 
      eluated from IVIG products, but it is less extensive than with unfractionated 
      IVIG.
CI  - Copyright (c) 2013 Elsevier B.V. All rights reserved.
FAU - Klaver, Andrea C
AU  - Klaver AC
AD  - Department of Neurology Research, Beaumont Health System, Royal Oak, MI, United 
      States. Electronic address: Andrea.Klaver@beaumont.edu.
FAU - Coffey, Mary P
AU  - Coffey MP
FAU - Smith, Lynnae M
AU  - Smith LM
FAU - Loeffler, David A
AU  - Loeffler DA
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130806
PL  - Netherlands
TA  - Immunol Lett
JT  - Immunology letters
JID - 7910006
RN  - 0 (Amyloid beta-Peptides)
RN  - 0 (Autoantibodies)
RN  - 0 (Complex Mixtures)
RN  - 0 (Immunoglobulins, Intravenous)
RN  - 0 (Peptide Fragments)
RN  - 0 (amyloid beta-protein (1-42))
SB  - IM
MH  - Alzheimer Disease/immunology/*therapy
MH  - Amyloid beta-Peptides/immunology
MH  - Antibody Affinity
MH  - Autoantibodies/*metabolism
MH  - Chemical Fractionation
MH  - Complex Mixtures/metabolism
MH  - Enzyme-Linked Immunosorbent Assay/*methods
MH  - Humans
MH  - Immunoglobulins, Intravenous/*metabolism/therapeutic use
MH  - Immunosorbent Techniques
MH  - Immunotherapy/*methods
MH  - Peptide Fragments/immunology
MH  - Protein Binding
OTO - NOTNLM
OT  - Abeta
OT  - Affinity chromatography
OT  - Antibody
OT  - Binding specificity
OT  - ELISA
OT  - Intravenous immunoglobulin
EDAT- 2013/08/10 06:00
MHDA- 2014/07/16 06:00
CRDT- 2013/08/10 06:00
PHST- 2013/06/25 00:00 [received]
PHST- 2013/07/25 00:00 [accepted]
PHST- 2013/08/10 06:00 [entrez]
PHST- 2013/08/10 06:00 [pubmed]
PHST- 2014/07/16 06:00 [medline]
AID - S0165-2478(13)00100-4 [pii]
AID - 10.1016/j.imlet.2013.07.008 [doi]
PST - ppublish
SO  - Immunol Lett. 2013 Jul-Aug;154(1-2):7-11. doi: 10.1016/j.imlet.2013.07.008. Epub 
      2013 Aug 6.