PMID- 6811171
OWN - NLM
STAT- MEDLINE
DCOM- 19821202
LR  - 20181130
IS  - 0009-9104 (Print)
IS  - 1365-2249 (Electronic)
IS  - 0009-9104 (Linking)
VI  - 48
IP  - 3
DP  - 1982 Jun
TI  - Anti-C1q column: ligand specific purification of immune complexes from human 
      serum or plasma. Analysis of the interaction between C1q and immune complexes.
PG  - 705-14
AB  - An efficient and reproducible procedure has been developed for the specific 
      isolation of immune complexes. PEG precipitation of EDTA serum or plasma was an 
      essential preliminary step to separate complex-bound from free C1q. PEG had no 
      discernible effect on the molecular weight size of the extracted complexes. 
      Redissolved complexes were incubated with a Sepharose-4B column coated with 
      anti-human C1q antibodies and following removal of unbound material the bound 
      complexes were sequentially eluted with 0.02 M EDTA, 0.5 M NaCl and 1 M propionic 
      acid. Characteristics of the affinity column were established by the purification 
      of 125I-labelled BSA-anti-BSA complexes and heat-aggregated IgG (HAGG) incubated 
      in normal human serum (NHS). EDTA and NaCl eluted complexes were of similar 
      molecular size and contained antigen, specific antibody, as well as human IgM, 
      IgG, albumin, C3, C3c, C3d and C1q. Acid eluted complexes contained the highest 
      yield of specific antigen and antibody and comprised in addition human C1q and 
      C3d. Activation of complement components after C1q made the bond between C1q and 
      immune complexes resistant to 0.5 M NaCl and interfered with the binding between 
      solid phase anti-C1q and complex bound C1q. Using BSA-anti-BSA complexes and HAGG 
      activated in NHS it was apparent that only a minority of the complexed material 
      was isolated via the C1q ligand and this probably applies to the C1q binding 
      assay. Most complexed material could be isolated using an anti-C3 affinity 
      column.
FAU - Kilgallon, W
AU  - Kilgallon W
FAU - Amlot, P L
AU  - Amlot PL
FAU - Williams, B D
AU  - Williams BD
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Clin Exp Immunol
JT  - Clinical and experimental immunology
JID - 0057202
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Complement C3)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Ligands)
RN  - 3WJQ0SDW1A (Polyethylene Glycols)
RN  - 80295-33-6 (Complement C1q)
RN  - EC 3.- (Complement Activating Enzymes)
SB  - IM
MH  - Antigen-Antibody Complex/immunology/*isolation & purification
MH  - Centrifugation, Density Gradient
MH  - Chromatography, Affinity
MH  - Complement Activating Enzymes/*immunology
MH  - Complement C1q
MH  - Complement C3/immunology
MH  - Hot Temperature
MH  - Humans
MH  - Immunodiffusion
MH  - Immunoglobulin G/immunology
MH  - Ligands
MH  - Methods
MH  - Polyethylene Glycols
PMC - PMC1536616
EDAT- 1982/06/01 00:00
MHDA- 1982/06/01 00:01
PMCR- 1983/06/01
CRDT- 1982/06/01 00:00
PHST- 1982/06/01 00:00 [pubmed]
PHST- 1982/06/01 00:01 [medline]
PHST- 1982/06/01 00:00 [entrez]
PHST- 1983/06/01 00:00 [pmc-release]
PST - ppublish
SO  - Clin Exp Immunol. 1982 Jun;48(3):705-14.