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. Following the same procedure, incubation separately of the above portions of the amyloid suspension and of the serum (each tube made up to same initial volume with normal saline) permitted calculation
Materials. Normal human serum was obtained from 13 healthy blood donors and two of the investigators.
FMF-serum was obtained from three patients suffering from familial Mediterranean fever (FMF), all of them with amyloidosis.
Denatured serum was prepared by heating at 100° for 15 min the sera obtained from three healthy blood donors and two of the investigators and collecting the supernatant after centrifugation in a Spinco model L at 30,000 rpm for 60 min.
Water-soluble amyloid was extracted separately by the method of Pras et al. 4 from the spleens obtained postmortem from a case of FMF and one of Hodgkins' disease.
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