Nuclease-coated bacteriophage: a sensitive tool for studying antigenic reactivity of synthetic sequence fragments |
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Authors: | S Fuchs M Sela C B Anfinsen |
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Affiliation: | Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel |
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Abstract: | Staphylococcal nuclease was conjugated to bacteriophage T4 using glutaraldehyde as a cross-linking agent. The conjugated phage is inactivated by antinuclease antibodies and this inactivation is specifically inhibited by nuclease in concentrations as low as 10?9m. Two fragments of the enzyme, namely P2 (residues 6–48) and P3 (residues 49–149) inhibit to a much lower extent the inactivation of the conjugated bacteriophage by the antibodies, than the native enzyme, but when mixed together (forming the noncovalent complex, nuclease-T), the inhibition curve obtained is similar to that obtained by native nuclease. This sensitive system was applied for testing different synthetic sequence fragments and for studying the complementarity of synthetic sequences in the P2 region with native P3. |
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