The purification and kinetic properties of biophosphoglycerate synthase from horse red blood cells.
Abstract: No abstract available
Publication Date: 1976-11-01 PubMed ID: 187124DOI: 10.1016/0003-9861(76)90438-0Google Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Cite This Article
APA
Rose AB, Dube S.
(1976).
The purification and kinetic properties of biophosphoglycerate synthase from horse red blood cells.
Arch Biochem Biophys, 177(1), 284-292.
https://doi.org/10.1016/0003-9861(76)90438-0 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Bisphosphoglycerate Mutase / blood
- Bisphosphoglycerate Mutase / isolation & purification
- Diphosphoglyceric Acids
- Erythrocytes / enzymology
- Horses
- Kinetics
- Phosphoglycerate Mutase / blood
- Phosphoric Monoester Hydrolases / blood
- Phosphotransferases / blood
Citations
This article has been cited 4 times.- Mulquiney PJ, Bubb WA, Kuchel PW. Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: in vivo kinetic characterization of 2,3-bisphosphoglycerate synthase/phosphatase using 13C and 31P NMR.. Biochem J 1999 Sep 15;342 Pt 3(Pt 3):567-80.
- Haggarty NW, Dunbar B, Fothergill LA. The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase.. EMBO J 1983;2(7):1213-20.
- Sasaki R, Chiba H. Role and induction of 2,3-bisphosphoglycerate synthase.. Mol Cell Biochem 1983;53-54(1-2):247-56.
- Joulin V, Peduzzi J, Roméo PH, Rosa R, Valentin C, Dubart A, Lapeyre B, Blouquit Y, Garel MC, Goossens M. Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence.. EMBO J 1986 Sep;5(9):2275-83.
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