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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Fujii, H. Yoshida, A. |
| Abstract | Inherited deficiency of phosphoglycerate kinase (PGK; ATP:3-phosphoglycerate 1-phosphotransferase, EC 2.7.2.3) is associated with chronic nonspherocytic hemolytic anemia and mental disorders in man. One such variant, PGK-Uppsala, was purified to homogeneity. PGK-Uppsala had a lower-than-normal specific activity (30% of normal in the backward reaction and about 20% of normal in the forward reaction) and higher-than-normal Michaelis constants for ATP, ADP, 3-phosphoglycerate and 1,3-diphosphoglycerate. Peptide mapping analysis revealed that the structural abnormality of PGK-Uppsala is a single amino acid substitution from arginine to proline at the 206th position. Based on the known complete amino acid sequence of the normal human PGK and the three-dimensional model deduced from horse PGK, correlations between the structural and functional abnormalities of PGK-Uppsala are discussed. Structural abnormalities of PGK-II, which is an electrophoretic variant not associated with enzyme deficiency, and PGK-München, which is associated with enzyme deficiency and heat instability but not associated with hemolytic anemia, are also discussed. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 77 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1980-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Anemia, Hemolytic, Congenital Nonspherocytic Enzymology Phosphoglycerate Kinase Genetics Amino Acid Sequence Electrophoresis, Polyacrylamide Gel Kinetics Peptide Fragments Deficiency Isolation & Purification Protein Conformation Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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