Sideroblastic anemia. Erythroid depression following transfusion.
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Biomedical subjects
Publications and source records attributed to E Beutler.
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A specific method for starch-gel electrophoresis of galactose-1-phosphate uridyltransferase has been developed. Electrophoresis of red-cell hemolyzate from normal subjects and subjects homozygous for the Duarte variant has shown that the Duarte variant has a slightly faster electrophoretic mobility than the normal enzyme under the various conditions used. Molecular-weight estimation on Sephadex G-200 indicates that this observed difference in electrophoreticmobility of the Duarte variant is not due to difference in molecular size. Both enzymes have a molecular weigh of approximately 85,000.
Starch-gel electrophoresis of extracts of human liver revealed the presence of a new hexose-6-phosphate dehydrogenase that was slower-moving at pH 8.6 than the sex-linked glucose-6-phosphate dehydrogenase. When the gel plate was stained, galactose-6-phos phate being used as a substrate, this enzyme band stained intensely, but the sex-linked glucose-6-phosphate dehydro genase failed to stain. This new human enzyme may well be homologous with the autosomally inherited glucose-6-phosphate dehydrogenase of the deer mouse (Peromyscus maniculatus), re ported by Shaw and Barto.
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