Ruminant cluster CD71
From a lysate of radiolabeled Theileria parva-infected bovine lymphocytes monoclonal antibody (mAb) IL-A77 immunoprecipitated a molecule of Mr 190 000 under non-reducing conditions, which was shown to be a homodimer of a Mr 90 000 protein after reduction (Naessens et al., 1996). Purification of the...
| Main Authors: | , |
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| Format: | Journal Article |
| Language: | Inglés |
| Published: |
Elsevier
1996
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10568/29860 |
| _version_ | 1855520695415472128 |
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| author | Naessens, Jan Davis, W.C. |
| author_browse | Davis, W.C. Naessens, Jan |
| author_facet | Naessens, Jan Davis, W.C. |
| author_sort | Naessens, Jan |
| collection | Repository of Agricultural Research Outputs (CGSpace) |
| description | From a lysate of radiolabeled Theileria parva-infected bovine lymphocytes monoclonal antibody (mAb) IL-A77 immunoprecipitated a molecule of Mr 190 000 under non-reducing conditions, which was shown to be a homodimer of a Mr 90 000 protein after reduction (Naessens et al., 1996). Purification of the bovine transferrin receptor using insoluble bovine transferrin revealed a band of the same Mr which could be bound by mAb IL-A77. Furthermore, the antibody could block binding of labeled bovine transferrin to immature erythroid cells from bone marrow. When cells were metabolically labeled, an additional band was observed when the receptor was precipitated from T. parva-infected lymphocytes, but not from concanavalin A (Con A) stimulated and cultured lymphocytes (Naessens et al., 1996). mAb IL-A165 could inhibit the binding of IL-A77 to T. parva-infected cells, suggesting it also detects transferrin receptor (Davis et al., 1996, this volume). |
| format | Journal Article |
| id | CGSpace29860 |
| institution | CGIAR Consortium |
| language | Inglés |
| publishDate | 1996 |
| publishDateRange | 1996 |
| publishDateSort | 1996 |
| publisher | Elsevier |
| publisherStr | Elsevier |
| record_format | dspace |
| spelling | CGSpace298602023-12-08T19:36:04Z Ruminant cluster CD71 Naessens, Jan Davis, W.C. ruminants biochemistry immunology From a lysate of radiolabeled Theileria parva-infected bovine lymphocytes monoclonal antibody (mAb) IL-A77 immunoprecipitated a molecule of Mr 190 000 under non-reducing conditions, which was shown to be a homodimer of a Mr 90 000 protein after reduction (Naessens et al., 1996). Purification of the bovine transferrin receptor using insoluble bovine transferrin revealed a band of the same Mr which could be bound by mAb IL-A77. Furthermore, the antibody could block binding of labeled bovine transferrin to immature erythroid cells from bone marrow. When cells were metabolically labeled, an additional band was observed when the receptor was precipitated from T. parva-infected lymphocytes, but not from concanavalin A (Con A) stimulated and cultured lymphocytes (Naessens et al., 1996). mAb IL-A165 could inhibit the binding of IL-A77 to T. parva-infected cells, suggesting it also detects transferrin receptor (Davis et al., 1996, this volume). 1996-08 2013-06-11T09:25:11Z 2013-06-11T09:25:11Z Journal Article https://hdl.handle.net/10568/29860 en Limited Access Elsevier Veterinary Immunology and Immunopathology;52(4): 257-258 |
| spellingShingle | ruminants biochemistry immunology Naessens, Jan Davis, W.C. Ruminant cluster CD71 |
| title | Ruminant cluster CD71 |
| title_full | Ruminant cluster CD71 |
| title_fullStr | Ruminant cluster CD71 |
| title_full_unstemmed | Ruminant cluster CD71 |
| title_short | Ruminant cluster CD71 |
| title_sort | ruminant cluster cd71 |
| topic | ruminants biochemistry immunology |
| url | https://hdl.handle.net/10568/29860 |
| work_keys_str_mv | AT naessensjan ruminantclustercd71 AT daviswc ruminantclustercd71 |