Isolation and partial characterization of monophosphoglycerate mutase from human erythrocytes.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. The isolation and partial characterization of diphosphoglycerate mutase from human erythrocytes
2. A reassessment of the phosphoglycerate bypass enzymes in human erythrocytes
3. Purification of Bisphosphoglyceromutase, 2, 3-Bisphosphoglycerate Phosphatase and Phosphoglyceromutase from Human Erythrocytes. Three Enzyme Activities in One Protein
4. Phosphate Transfer between 2,3-Bisphosphoglycerate and Monophosphoglycerate Catalyzed by Bisphosphoglycerate Phosphatase
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1. Functional characterization of two members of histidine phosphatase superfamily in Mycobacterium tuberculosis;BMC Microbiology;2013-12
2. Characterization of the first described mutation of human red blood cell phosphoglycerate mutase;Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease;2005-06
3. Purification and properties of the phosphoglycerate mutase isozymes from the mouse;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1985-01
4. Evidence for the presence of a hybrid of phosphoglyceromutase/bisphosphoglyceromutase in the red cells: Partial characterization of the hybrid;Biochemical and Biophysical Research Communications;1984-05
5. Purification of human erythrocyte phosphoglyceromutase;Journal of Chromatography A;1984-01
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