Acquired erythroenzymopathy in a monozygotic twin with acute myeloid leukemia.
The specific activity of several red cell enzymes was studied in a pair of monozygotic twins, one of whom presented acute myeloblastic leukemia. When the intrapair variation of these twins was compared with that of a series of nine normal twins, a significant decrease in phosphoglycerate kinase, diphosphoglycerate mutase, pyruvate kinase, lactic dehydrogenase, adenylate kinase and glucose-6-phosphate dehydrogenase activities and an increase in 6-phosphogluconate dehydrogenase activity were demonstrable for the leukemic twin. The heat stability of the leukemic proband's pyruvate kinase at pH 8.0 and 56 degrees C was less than that of the normal twin, suggesting an acquired qualitative disorder.
D000262:Adenylyl Cyclases / Q000097:blood; D000328:Adult; D001731:Bisphosphoglycerate Mutase / Q000097:blood; D004200:Diseases in Twins; D004912:Erythrocytes / Q000201:enzymology*; D005260:Female; D005954:Glucosephosphate Dehydrogenase / Q000097:blood; D006801:Humans; D007770:L-Lactate Dehydrogenase / Q000097:blood; D015470:Leukemia, Myeloid, Acute / Q000201:enzymology* / Q000235:genetics; D010735:Phosphoglycerate Kinase / Q000097:blood; D011770:Pyruvate Kinase / Q000097:blood*; D014430:Twins, Monozygotic
D007770:L-Lactate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D011770:Pyruvate Kinase; D010735:Phosphoglycerate Kinase; D000262:Adenylyl Cyclases; D001731:Bisphosphoglycerate Mutase