Characterization of a human interleukin 1 inhibitor

Abstract

Human urine contains a specific inhibitor of interleukin 1 (IL 1) that is found in increased amounts during fever. This inhibitor was purified by using a sequence of ammonium sulfate fractionation, DEAE cellulose ion-exchange chromatography, molecular sieve chromatography on Sephacryl S-200, affinity chromatography on concanavalin A (Con A) Sepharose, and polyacrylamide gel electrophoresis. Two peaks of IL 1 inhibitory material were eluted from the polyacrylamide gels. One peak contained three proteins of 29, 32, and 67 kd, respectively, which could be visualized by silver staining. The second peak contained only a small amount of the 67 kd protein. A partially purified inhibitor fraction was found to cross-react with antisera directed against two low m.w. urine trypsin inhibitors that are cleavage products of the serum inter-alpha-trypsin inhibitor. Although these findings suggest that the urine IL 1 inhibitor may be related to the inter-alpha-trypsin inhibitor, a more exact identification will require either a homogeneous inhibitor preparation or a monospecific antiserum.