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Antibody response in immunized rabbits measured with bacterial immunoglobulin-binding proteins

Elbashir, M I (author)
Lund University
Nilson, B H (author)
Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,SEBRA Sepsis and Bacterial Resistance Alliance,Forskargrupper vid Lunds universitet,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine,Lund University Research Groups
Akesson, P (author)
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Björck, L (author)
Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Molekylär patogenes,Forskargrupper vid Lunds universitet,epIgG,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Molecular Pathogenesis,Lund University Research Groups
Akerström, B (author)
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 (creator_code:org_t)
Elsevier BV, 1990
1990
English.
In: Journal of Immunological Methods. - : Elsevier BV. - 0022-1759. ; 135:1-2, s. 9-171
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Protein G, an immunoglobulin (Ig)-binding protein isolated from group C or G streptococci, binds to the Fc portion of IgG. Protein L, from the anaerobic bacterium Peptostreptococcus magnus, specifically binds light chains of Ig. In this study, protein G and L were used to measure the production of antibodies in immunized rabbits. Two rabbits were immunized with a mixture of human urinary proteins from a patient with tubular proteinuria, and blood samples were collected regularly from the animals for 6 weeks after the immunization. The antibody levels of the blood samples against six of the proteins in the antigen mixture were then measured by ELISA. Microtiter plates were coated with each of the antigens, incubated with the rabbit serum samples, and the specific antibodies of the IgG class measured by incubation with biotinylated protein G, and antibodies of all Ig classes with biotinylated protein L. Alternatively, Western blotting was employed, where the antibodies which bound to each antigen after separation by SDS-PAGE and transfer to nitrocellulose membranes, were detected by protein G or L. The results showed that antibody production against five of the antigens, albumin, alpha 1 gamma-acid glycoprotein, alpha 1 gamma-microglobulin, Ig light chains, and retinol-binding protein, showed a similar pattern, although the magnitude of the initial IgM response differed somewhat. After 6 weeks, the levels of the protein G-binding antibodies had reached a plateau, while those of protein L-binding antibodies were still increasing. The response to the sixth antigen, beta 2 microglobulin, was considerably different. A dramatic increase of anti-beta 2 gamma-microglobulin antibodies was seen during the 4th week after immunization when protein L was used.

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)

Keyword

Animals
Antibody Formation
Bacterial Proteins
Biotin
Blotting, Western
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Immunization
Immunoglobulin Fc Fragments
Immunologic Techniques
Proteins
Proteinuria
Rabbits
Journal Article
Research Support, Non-U.S. Gov't

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Elbashir, M I
Nilson, B H
Akesson, P
Björck, L
Akerström, B
About the subject
MEDICAL AND HEALTH SCIENCES
MEDICAL AND HEAL ...
and Basic Medicine
and Immunology in th ...
Articles in the publication
Journal of Immun ...
By the university
Lund University

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