Blue dextran-sepharose: an affinity column for the dinucleotide fold in proteins.
- 1 February 1975
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 72 (2) , 669-672
- https://doi.org/10.1073/pnas.72.2.669
Abstract
A procedure is described to utilize blue dextran-Sepharose as an affinity chromatographic column specific for the super-secondary structure called the dinucleotide fold, which forms the binding sites for substrates and effectors on a wide range of proteins. The procedure can be used to identify proteins, either purified or in crude cellular extracts, that possess the dinucleotide fold and to significantly improve the purification procedures for those proteins that possess the fold.Keywords
This publication has 32 references indexed in Scilit:
- The Structure of Ferrocytochrome c at 2.45 A ResolutionJournal of Biological Chemistry, 1973
- Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome cJournal of Molecular Biology, 1973
- Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0 Å resolutionJournal of Molecular Biology, 1972
- Wechselwirkungen der Hefe‐Phosphofructokinase mit Dextranblau 2000European Journal of Biochemistry, 1971
- Interaction of lactate dehydrogenase with its coenzyme, nicotinamide-adenine dinucleotideJournal of Molecular Biology, 1970
- The structure of the nicotinamide-adenine dinucleotide coenzyme when bound to lactate dehydrogenaseJournal of Molecular Biology, 1970
- Binding of phosphate ligands to ribonuclease ABiochemistry, 1968
- Purification of Escherichia coli phosphofructokinaseBiochemical and Biophysical Research Communications, 1967
- BINDING OF NUCLEOTIDES AND CALCIUM TO EXTRACELLULAR NUCLEASE OF STAPHYLOCOCCUS AUREUS - STUDIES BY GEL FILTRATION1967
- Fluorescence Spectra and Polarization of Glyceraldehyde-3-phosphate and Lactic Dehydrogenase Coenzyme ComplexesJournal of Biological Chemistry, 1958