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 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).

Bibliographic Details

Main Authors:	Naessens, Jan, Davis, W.C.
Format:	Journal Article biblioteca
Language:	English
Published:	Elsevier 1996-08
Subjects:	ruminants, biochemistry, immunology,
Online Access:	https://hdl.handle.net/10568/29860 https://doi.org/10.1016/0165-2427(96)05572-9
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