Abstract
In systemic amyloidosis, the rare instances of recovery following the successful treatment of a predisposing disease present a challenge in the management of an otherwise fatal disorder 1,2. Notwithstanding, experimental endeavor has been directed largely toward unravelling the nature of amyloid and its pathogenesis rather than the biological mechanism by which this fibrillar protein may be removed from the tissues 3. The following experiments indicate that normal human serum contains a heat-stable component capable of degrading amyloid in vitro.Procedure. In principle, one portion of a standard suspension of water-soluble amyloid 4 was incubated with two portions of human serum in a test tube for 2 hr at 37°. Following incubation the precipitate obtained by centrifugation for 30 min in a cooled PC-2 Sorvall Centrifuge at 15,000 rpm was collected, twice washed in cold saline, and recentrifuged as above, resuspended in normal saline, and its total protein content determined by the Biuret method at 555 nm. ...
Published Version
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