Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules
Three bacterial species of Clostridium (septicum, tertium and sporogenes) were identified to produce extracellular proteases cleaving IgA to Fab and Fc fragments, as demonstrated by SDS-PAGE and immunoelectrophoretic procedures. These enzymes acted on monometric IgA1 paraproteins and normal serum Ig...
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Wiley
1991
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| Online Access: | http://eprints.um.edu.my/280/ http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1384471/?tool=pubmed |
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| author | Hashim, Onn Haji Hassan, H. |
| author_facet | Hashim, Onn Haji Hassan, H. |
| author_sort | Hashim, Onn Haji |
| building | UM Library |
| collection | Institutional Repository |
| content_provider | Universiti Malaya |
| content_source | UM Research Repository |
| continent | Asia |
| country | Malaysia |
| description | Three bacterial species of Clostridium (septicum, tertium and sporogenes) were identified to produce extracellular proteases cleaving IgA to Fab and Fc fragments, as demonstrated by SDS-PAGE and immunoelectrophoretic procedures. These enzymes acted on monometric IgA1 paraproteins and normal serum IgA1 but had no activity on IgA2 paraproteins and intact secretory IgA1 from human colostrum. Their action on polyclonal serum IgA1 suggested the absence of neutralizing anti-clostridial IgA protease activity. Although the enzymes were shown not to act on secretory IgA1, they were, however, able to digest free alpha-heavy chains of the dimeric IgA molecules. Susceptibility of the alpha-heavy chain to the proteases was more likely due to the change to a more accessible conformation than because of the absence of neutralizing anti-enzymic activity. |
| format | Article |
| id | my.um.eprints-280 |
| institution | Universiti Malaya |
| publishDate | 1991 |
| publisher | Wiley |
| record_format | eprints |
| spelling | my.um.eprints-2802025-04-10T01:03:08Z http://eprints.um.edu.my/280/ Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules Hashim, Onn Haji Hassan, H. R Medicine (General) Three bacterial species of Clostridium (septicum, tertium and sporogenes) were identified to produce extracellular proteases cleaving IgA to Fab and Fc fragments, as demonstrated by SDS-PAGE and immunoelectrophoretic procedures. These enzymes acted on monometric IgA1 paraproteins and normal serum IgA1 but had no activity on IgA2 paraproteins and intact secretory IgA1 from human colostrum. Their action on polyclonal serum IgA1 suggested the absence of neutralizing anti-clostridial IgA protease activity. Although the enzymes were shown not to act on secretory IgA1, they were, however, able to digest free alpha-heavy chains of the dimeric IgA molecules. Susceptibility of the alpha-heavy chain to the proteases was more likely due to the change to a more accessible conformation than because of the absence of neutralizing anti-enzymic activity. Wiley 1991-06 Article PeerReviewed Hashim, Onn Haji and Hassan, H. (1991) Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules. Immunology, 73 (2). pp. 235-8. ISSN 0019-2805, DOI 2071167. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1384471/?tool=pubmed 2071167 |
| spellingShingle | R Medicine (General) Hashim, Onn Haji Hassan, H. Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules |
| title | Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules |
| title_full | Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules |
| title_fullStr | Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules |
| title_full_unstemmed | Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules |
| title_short | Actions of three clostridial IgA proteases on distinct forms of immunoglobulin A molecules |
| title_sort | actions of three clostridial iga proteases on distinct forms of immunoglobulin a molecules |
| topic | R Medicine (General) |
| url | http://eprints.um.edu.my/280/ http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1384471/?tool=pubmed |
| url_provider | http://eprints.um.edu.my/ |