Specificity of human natural antibody to recombinant tissue-type plasminogen activator (t-PA) expressed in mouse C127 cells.
A natural antibody with binding specificity for recombinant tissue-type plasminogen activator (t-PA) expressed in mouse C127 cells was present in almost all disease-free humans and patients with thrombotic disease examined. This antibody was specific for a carbohydrate, alpha 1-3-linked galactose residue, and was isolated by affinity chromatography using Synsorb 90 coupled with the glycosidic epitope Gal alpha 1-3Gal beta 1-4Glc-R as an immunoadsorbent. The evaluation of various glycoproteins for ability to bind the purified antibody in ELISA demonstrated that not only recombinant t-PA from C127 cells but also recombinant erythropoietin (EPO) and recombinant protein C produced in C127 cells have alpha 1-3-linked galactose residues on their sugar side chains. This anti-alpha-galactosyl antibody also interacted with natural t-PA from human vascular trees (vascular t-PA) and placenta (placenta t-PA), but not to melanoma t-PA, recombinant t-PA, EPO or protein C expressed in Chinese hamster ovary (CHO) cells.
Tsuji
J
J
Research Institute, Toyobo Co., Ltd., Shiga, Japan.
Noma
S
S
Suzuki
J
J
Okumura
K
K
Shimizu
N
N
D000818:Animals; D000918:Antibody Specificity; D002460:Cell Line; D006801:Humans; D051379:Mice; D011994:Recombinant Proteins / Q000276:immunology; D010959:Tissue Plasminogen Activator / Q000276:immunology*
D011994:Recombinant Proteins; D010959:Tissue Plasminogen Activator