Structure-Disrupting Ions: Detection of Qualitative Change in an Enzyme
- 27 May 1966
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 152 (3726) , 1245-1246
- https://doi.org/10.1126/science.152.3726.1245
Abstract
Preparations of erythrocyte glucose-6-phosphate dehydrogenase from normal individuals show similar degrees of inhibition by neutral salts. Preparations from Caucasian subjects with different hereditary deficiency syndromes differ from each other and from normal subjects, indicating a qualitative difference in these specific "deficient" enzymes. Sensitivity to neutral salts may be a means of detecting an amino acid substitution.This publication has 9 references indexed in Scilit:
- The Effect of Structure-disrupting Ions on the Activity of Myosin and Other EnzymesJournal of Biological Chemistry, 1966
- Neutral Salts: The Generality of Their Effects on the Stability of Macromolecular ConformationsScience, 1964
- Functionally Abnormal Glucose-6-Phosphate DehydrogenasesCold Spring Harbor Symposia on Quantitative Biology, 1964
- SEX-LINKED ELECTROPHORETIC DIFFERENCE IN GLUCOSE-6-PHOSPHATE DEHYDROGENASE1963
- Glucose 6-Phosphate Dehydrogenase from Human ErythrocytesPublished by Elsevier ,1962
- Glucose 6-Phosphate Dehydrogenase from Human ErythrocytesPublished by Elsevier ,1962
- GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM HUMAN ERYTHROCYTES .2. SUBACTIVE STATES OF ENZYME FROM NORMAL PERSONS1962
- DIFFERENT ENZYMIC EXPRESSIONS OF MUTANTS OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASEProceedings of the National Academy of Sciences, 1960
- The nature of enzyme inhibitions in bacterial luminescence: Sulfanilamide, urethane, temperature and pressureJournal of Cellular and Comparative Physiology, 1942