Presence of Glycoproteins in Secondary Amyloid Deposits Related to Serum Glycoprotein

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Abstract
Summary By means of alcohol fractionation on tissues from subjects with secondary amyloidosis and on normal tissue two fractions of glycoprotein were obtained, namely one fraction of ground substance origin and another with serum glycoprotein properties. These two fractions were analyzed for total non-hexosamine protein-bound hexose and a marked increase in total protein-bound hexose was demonstrated in these two. fractions of the amyloid kidneys and spleens, as compared with the normals. In the liver no difference was seen between amyloid and normal. That the amyloid substance is a mixture of different glycoproteins is shown by these findings, and that the greater part of this increase is not of ground-substance origin is indicated by the fact that about two thirds of the amyloid substance was a non-glucuronic acid containing periodic acid-Schiff stainable glycoproteins of a serum glycoprotein nature which showed no signs of metachromasia and migrated as alpha-2 beta globulin on paper electrophoresis.

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