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Search: (AMNE:(MEDICIN OCH HÄLSOVETENSKAP Medicinska och farmaceutiska grundvetenskaper Immunologi inom det medicinska området)) > (1980-1989) > Protein HC-IgA comp...

Protein HC-IgA complexes carry antibody activities

Truedsson, L (author)
Lund University,Lunds universitet,Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Microbiology, Immunology and Glycobiology - MIG,Department of Laboratory Medicine,Faculty of Medicine,Skåne University Hospital
Grubb, A (author)
Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Cystatin C, njursjukdom, amyloidos och antibiotika,Forskargrupper vid Lunds universitet,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine,Cystatin C, renal disease, amyloidosis and antibiotics,Lund University Research Groups,Skåne University Hospital
 (creator_code:org_t)
Wiley, 1988
1988
English.
In: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 27:2, s. 201-208
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Polyclonal protein HC-IgA complexes (HC-IgA) were isolated from two different serum pools. Their hydrodynamic volumes were found to be slightly greater than that of monomeric IgA but less than that of dimeric IgA. Sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis of reduced and carboxymethylated complexes followed by immunoblotting showed that the complexes contained normal light and heavy Ig chains, and one polypeptide chain with Mr = 90,000, which carried both IgA alpha chain and protein HC epitopes. Enzyme-linked immunosorbent assays (ELISA) demonstrated that the isolated HC-IgA carried about 0.1 and 4%, respectively, of the antibody activities against one carbohydrate antigen (Yersinia enterocolitica serotype 0:3 lipopolysaccharide) and one protein antigen (rabbit IgG, i.e. antigen for rheumatoid factors) of the IgA populations of the two serum pools. HC-IgA with rheumatoid factor activity could also be demonstrated in the unfractionated serum pool. The binding of HC-IgA in the ELISA was not mediated through its protein HC part. The present observations show that HC-IgA carries antibody activities and constitutes a unique class of IgA complexes, since it does not dissociate under denaturating conditions after reduction. It may represent a further biological potential of the humoral immune system.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Immunology in the medical area (hsv//eng)
MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin -- Reumatologi och inflammation (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine -- Rheumatology and Autoimmunity (hsv//eng)
MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Microbiology in the medical area (hsv//eng)

Keyword

Alpha-Globulins/isolation & purification
Antibodies/physiology
Enzyme-Linked Immunosorbent Assay
Humans
Immunoglobulin A/isolation & purification
Rheumatoid Factor/immunology

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Truedsson, L
Grubb, A
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