Purification and Characterization of Two High-Affinity (Adenosine 3',5'-Monophosphate)-Binding Proteins from Yeast. Identification as Multiple Forms of Glyceraldehyde-3-Phosphate Dehydrogenase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1980.tb04765.x/fullpdf
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4. An Adenosine 3':5'-Monophosphate/Adenosine Binding Protein from Mouse Liver. A Study of Its Interaction with Synthetic and Naturally Occurring Adenosine Derivatives
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1. Cyclic AMP affinity purification and ESI-QTOF MS-MS identification of cytosolic glyceraldehyde 3-phosphate dehydrogenase and two nucleoside diphosphate kinase isoforms from tobacco BY-2 cells;FEBS Letters;2001-10-30
2. Glyceraldehyde-3-phosphate dehydrogenase;Enzyme Handbook;1993
3. Purification and Immunological Properties of NAD-Dependent Glyceraldehyde-3-Phosphate Dehydrogenase from the Plant Cytosol of Nitrogen Fixing Soybean Nodules;Journal of Plant Physiology;1991-05
4. Specific, high-affinity binding sites for human luteinizing hormone (hLH) and human chorionic gonadotrophin (hCG) in candida species;Biochemical and Biophysical Research Communications;1990-03
5. Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver as derived from the cDNA sequence.;Proceedings of the National Academy of Sciences;1987-02-01
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