The limited proteolysis of tumor necrosis factor-α |
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Authors: | Linda Owers Narhi Michael F Rhode Pamela Hunt and Tsutomu Arakawa |
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Institution: | (1) Amgen Inc., 1900 Oak Terrace Lane, 91320 Thousand Oaks, California |
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Abstract: | The limited proteolysis of human recombinant TNF- by trypsin yields two stable products resulting from cleavage after Arg6 and Arg44. In solution these two products remain associated together in a trimer with a Stokes' radius slightly greater than the radius of intact TNF- and, therefore, could not be separated from each other under nondenaturing conditions. This limited digest retains at least 20% of the activity of the original TNF- sample, and has a tertiary structure that is similar to that of the native protein by circular dichroism. On the other hand, incorrectly folded, inactive TNF- undergoes extensive digestion following similar treatment with trypsin. These results indicate that the active form of TNF- has a tight core structure which is maintained afterN-terminal cleavage and removal. |
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Keywords: | Tumor necrosis factor-" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0"> limited proteolysis |
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