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Conformational change of mastoparan from wasp venom on binding with phospholipid membrane |
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| Authors: | T Higashijima K Wakamatsu M Takemitsu M Fujino T Nakajima T Miyazawa |
| Affiliation: | Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England |
| Abstract: | Aglycosylated IgG produced by hybridoma cells cultured in the presence of tunicamycin was compared with normal IgG for its ability to bind to staphylococcal protein A. No differences were found in binding or elution profiles. It is concluded that aglycosylation does not produce major structural alterations at the CH2-CH3 interface of the Fc region of IgG. |
| Keywords: | Mouse IgG2a Staphylococcal protein A Tunicamycin Role of carbohydrate Aglycosylation IgG secondary function DNP 2,4-dinitrophenyl BSA bovine serum albumin FCS foetal calf serum PBS phosphate buffered saline SDS-PAGE sodium dodecyl sulphate polycrylamide gel electrophoresis CPB citrate-phosphate buffer containing BSA |
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