title: Platelet membrane studies in the May-Hegglin anomaly.
abstract: Since studies of the giant platelets in the Bernard-Soulier syndrome have shown decreased electrophoretic mobility, decreased sialic acid, and an abnormality in a membrane glycoprotein, we performed similar studies on the giant platelets from two patients with the May-Hegglin anomaly. The patients' platelet electrophoretic mobilities did not differ from control. Although the total sialic acid contents of the patients' platelets were greater than control when calculated per platelet, they were very similar to control when normalized for differences in platelet volume and surface area. When platelet proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis there were no differences between the glycoproteins of control and patient platelets as judged by the patterns of periodic acid Schiff staining and fluorescein-labeled concanavalin A binding. Similarly, patterns of surface glycoprotein labeling by neuraminidase/galactose oxidase/KB3H4 were identical. We conclude that unlike the giant platelets in the Bernard-Soulier syndrome, those of the May-Hegglin anomaly are not associated with a membrane abnormality detectable by these techniques.
mesh_terms: D000328:Adult; D001791:Blood Platelet Disorders / Q000097:blood*; D001792:Blood Platelets / Q000166:cytology; D001798:Blood Proteins; D002462:Cell Membrane; D004586:Electrophoresis; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005692:Galactose Oxidase; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D009439:Neuraminidase; D012794:Sialic Acids
chemical_list: D001798:Blood Proteins; D008565:Membrane Proteins; D012794:Sialic Acids; D005692:Galactose Oxidase; D009439:Neuraminidase