Antibodies directed against the thiomannose moiety of a glycoconjugate of 2-imino-2-methoxyethyl 1-thio-alpha-D-mannopyranoside and bovine serum albumin |
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Authors: | John H Pazur Belin Liu Nan Q Li and Yuan Chan Lee |
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Institution: | (1) Paul M. Althouse Laboratory, The Pennsylvania State University, 16802 University Park, Pennsylvania;(2) Present address: Chengdu University of Science and Technology, Chengdu, China;(3) Department of Biology and McCollum-Pratt Institute, The John Hopkins University, 21218 Baltimore, Maryland |
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Abstract: | Anti-thiomannose antibodies were induced in rabbits immunized with a glycoconjugate of 2-imino-2-methoxyethyl 1-thio- -d-mannopyranoside (Man-S) and bovine serum albumin (BSA). Also anti-BSA antibodies directed against the BSA moiety of the glycoconjugate were detected in low concentrations in the immune serum. However, antibodies against the combinatorial epitope of the hapten group and the carrier protein were not detected. The anti-thiomannose and the anti-BSA antibodies were isolated in pure forms by affinity chromatography on Sepharose 4B-bearing thiomannosyl-BSA ligands or BSA ligands. The anti-thiomannose antibodies constituted the major fraction of the antibodies, and these antibodies were isolated in pure form for the first time. The specificity of the thiomannose antibodies was established from data of experiments of periodate oxidation, perpropionic acid oxidation, hapten inhibition, and agar diffusion. Isoelectrofocusing showed that the anti-thiomannose antibody preparation consisted of at least six isomeric proteins, all of which exhibited antibody activity against the glycoconjugate of thiomannose and BSA. |
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Keywords: | Glycoconjugate thiomannose-bovine serum albumin anti-thiomannose antibodies affinity chromatography isoelectrofocusing |
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