Tryptophan residues of IgGRF from rheumatoid arthritis patient were modified with N-Bromosuccinimide (NBS) and the product of modification was characterized by UV-spectrum、Fluorescence emission spectrum and CD-spectr...Tryptophan residues of IgGRF from rheumatoid arthritis patient were modified with N-Bromosuccinimide (NBS) and the product of modification was characterized by UV-spectrum、Fluorescence emission spectrum and CD-spectrum. The corresponding adsorption capacity of immobilized ssDNA immunoadsorbent for IgGRF was enhanced from 46% to 86%, This result indicates the tryptophan residue is essential for the interaction between ssDNA and IgGRF .and ionic-bonding plays an important role in adsorption.展开更多
Rheumatoid factors(RFs) are the characteristic autoantibodies of rheumatoid arthritis. Recent researches in our laboratory showed that the immobilized single-stranded DNA(ss-DNA) immunoadsorbent can selectively remove...Rheumatoid factors(RFs) are the characteristic autoantibodies of rheumatoid arthritis. Recent researches in our laboratory showed that the immobilized single-stranded DNA(ss-DNA) immunoadsorbent can selectively remove RFs from the serum of patients. In the present paper are studied the modification of argininine, tryptophan, lysine residues and carboxyl terminus of IgGRF, which was separated from patients′ serum, with 1,2-cyclohexanedione(CHD), N-bromosuccinimide(NBS), pyridoxal 5′-phosphate(PP) and 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide(EDC) respectively, and their effects on the adsorption capacity of the immobilized ss-DNA immunoadsorbent for IgGRF. After the specific modification, the corresponding adsorption capacities of the adsorbents were changed from 48%, 46%, 44% and 54% to 84%, 14%, 21% and 81%, respectively. These results indicate that the electrostatic or ionic-bonding is essential for the interaction between ss-DNA and IgGRF.展开更多
基金National Basic Science and Development of China (G1999O64707)
文摘Tryptophan residues of IgGRF from rheumatoid arthritis patient were modified with N-Bromosuccinimide (NBS) and the product of modification was characterized by UV-spectrum、Fluorescence emission spectrum and CD-spectrum. The corresponding adsorption capacity of immobilized ssDNA immunoadsorbent for IgGRF was enhanced from 46% to 86%, This result indicates the tryptophan residue is essential for the interaction between ssDNA and IgGRF .and ionic-bonding plays an important role in adsorption.
基金Key Projectof National Basic Science and Developm ent(No.G19990 6 4 70 7) and Tianjin- Nankai U niversi-ty Co- Construction Foundation and China- UK Collaboration Project
文摘Rheumatoid factors(RFs) are the characteristic autoantibodies of rheumatoid arthritis. Recent researches in our laboratory showed that the immobilized single-stranded DNA(ss-DNA) immunoadsorbent can selectively remove RFs from the serum of patients. In the present paper are studied the modification of argininine, tryptophan, lysine residues and carboxyl terminus of IgGRF, which was separated from patients′ serum, with 1,2-cyclohexanedione(CHD), N-bromosuccinimide(NBS), pyridoxal 5′-phosphate(PP) and 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide(EDC) respectively, and their effects on the adsorption capacity of the immobilized ss-DNA immunoadsorbent for IgGRF. After the specific modification, the corresponding adsorption capacities of the adsorbents were changed from 48%, 46%, 44% and 54% to 84%, 14%, 21% and 81%, respectively. These results indicate that the electrostatic or ionic-bonding is essential for the interaction between ss-DNA and IgGRF.
