Abstract
Summary
1. Euglobulins were prepared by 3 different methods from“latex positive” pooled serum. 2. Total protein bound hexoses, glucosamine, and sialic acid were measured on each euglobulin preparation. All were somewhat similar with the exception of the euglobulin prepared with hydrochloric acid, which had a higher per cent of hexose to protein. All showed marked increase in content when compared with euglobulins isolated from a pooled “latex negative” normal serum. 3. Paper electrophoretic examination reveals proteins that migrate as gamma globulins and are highly PAS positive. 4. A uronic acid-containing mucopolysaccharide was isolated from the cold agglutinating euglobulin.
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