Formation of active phosphoenzymes with the diphosphoglycerate-dependant phosphoglycerate mutases
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چکیده
منابع مشابه
Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?
It has been reported [Smith, McWilliams & Hass (1986) Biochem. Biophys. Res. Commun. 136, 336-340] that addition of certain metal ions, notably Co2+ and Mn2+, promoted the refolding of denatured phosphoglycerate mutase from wheat germ. We have re-investigated these experiments and have shown that, when precautions are taken to avoid artefacts in the assay system, the metal ions do not promote a...
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abstract because of the many geopolitical, geo economical and geo strategically potentials and communicational capabilities of eco region, members can expand the convergence and the integration in base of this organization that have important impact on members development and expanding peace in international and regional level. based on quality analyzing of library findings and experts interv...
15 صفحه اولThe active site of yeast phosphoglycerate mutase.
Amdt, U. W., Champness, J. N., Phizackerley, R. P. & Wonawtt, A. J. (1973)J. Appl. Crystallogr. 6,457-463 Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Pogson, C. I., Wilson, I. A,. Corran, P. H., Furth, A. J., Milman, J. D., Offord, R. E., Priddle, J. D. & Whaley, S. G. (1975) Nature (London) 255,609-614 Harkins, R. N. & Fothergill, L. A. (1977) Biochem. SOC. Trans. 5,772-774 ...
متن کاملThe Journal of Biological Chemistry
A very rapid procedure for the preparation of phosphoglycerate mutase from chicken breast muscle is presented. Commercially available frozen chicken breasts may be used. The enzyme is obtained in high yields, and the specific activity of the crystalline homogenous preparations is equal to that of the crystalline enzymes from yeast and rabbit muscle. The chicken breast enzyme requires 2,3-diphos...
متن کاملPhosphoglycerate Mutases Function as Reverse Regulated Isoenzymes in Synechococcus elongatus PCC 7942
Phosphoglycerate-mutase (PGM) is an ubiquitous glycolytic enzyme, which in eukaryotic cells can be found in different compartments. In prokaryotic cells, several PGMs are annotated/localized in one compartment. The identification and functional characterization of PGMs in prokaryotes is therefore important for better understanding of metabolic regulation. Here we introduce a method, based on a ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1280100pa