Amyloid 'degrading factor activity': a non-specific XXXX -mediated effect.

@entity1 @entity2313 @entity5066 @entity1098 @entity102 @entity1582 @entity460 @entity309 @entity1760
The clarification of turbid AA-amyloid-fibril-containing agarose gels by serum has been ascribed to degradation of the fibrils and designated as 'amyloid degrading factor'. In the present study, sera of 32 healthy blood donors and 32 @entity1 with @entity309 all showed 'degrading factor activity' against both @entity5066 fibrils and a non-fibrillar reticulin preparation of normal liver in an agarose plate assay. @entity1582 fibrils were not affected. The 'degrading activity' of serum was correlated with the serum @entity2313 concentration, and the effect was also given by purified @entity1 and bovine serum @entity2313 , although it was not seen with other serum proteins. The 'degrading activity' of serum against @entity5066 and reticulin was significantly correlated: both substrates showed low levels in a @entity102 such as @entity309 , and reticulin inhibited 'degrading activity' against @entity5066 . These results suggest the same process involves both substrates. 'Degrading activity' was also given by @entity1098 and a specific @entity460 chelator, and was inhibited by @entity460 and @entity1760 . An enzyme inhibitor showed only partial inhibition of the 'degrading activity' of serum, purified @entity2313 , and @entity1098 . These results suggest that serum 'degrading factor activity' is a non-specific @entity460 -mediated effect against @entity5066 and reticulin preparations dispersed in agarose. It may represent a change in the degree of aggregation of these proteins rather than being an effect of proteolytic degradation. This confirms the conclusions of other workers that amyloid 'degrading factor activity' is an phenomenon in vitro of doubtful pathophysiological significance.
