MALLORY BODIES - ISOLATION OF HEPATOCELLULAR HYALIN AND ELECTROPHORETIC RESOLUTION OF POLYPEPTIDE COMPONENTS

Abstract

Mallory bodies (MB) were obtained in purified form from human liver obtained at autopsy from patients with alcoholic liver disease using a new procedure consisting of sedimentation through a Ficoll viscosity barrier. Preparations from 6 livers ranged in purity from 95-99%. MB preparations were autofluorescent. MB were strongly agglutinated by concanavalin A. The presence of carbohydrate was also indicated by the fact that MB bound fluorescently labeled concanavalin A; no binding was observed in the presence of appropriate inhibitor monosaccharides. Direct analysis indicated that MB contained variable amounts of neutral hexose (0.65-2.4 .mu.mol of glucose-equivalents/mg protein) but no sialic acid. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that purified MB contain 5 major polypeptides possessing apparent MW of 56,000, 48,500-45,000 (triplet) and 32,500. Periodic acid-Schiff-positive components were not detected. Scanning electron microscopy of isolated MB revealed the presence of a rough, fibrous surface, whereas conventional transmission electron microscopy indicated the filamentous nature of MB.