The purification of porcine heart lactate dehydrogenase by affinity chromatography
Author:
Funder
American Cancer Society
National Science Foundation
National Institutes of Health
Publisher
Elsevier BV
Reference5 articles.
1. Affinity chromatography of lactate dehydrogenase Model studies demonstrating the potential of the technique in the mechanistic investigation as well as in the purification of multi-substrate enzymes
2. The resolution of some steps of the reactions of lactate dehydrogenase with its substrates
3. The separation of lactate dehydrogenase X from other lactate dehydrogenase isozymes of mouse testes by affinity chromatography
4. The use of ternary complexes to study ionizations and isomerizations during catalysis by lactate dehydrogenase
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1. The use of selective adsorbents in capillary electrophoresis-mass spectrometry for analyte preconcentration and microreactions: A powerful three-dimensional tool for multiple chemical and biological applications;ELECTROPHORESIS;2001-09
2. Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site.;Journal of Biological Chemistry;1992-04
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5. The reactions of pyridoxal 5′-phosphate with the M4 and H4 isoenzymes of pig lactate dehydrogenase;Archives of Biochemistry and Biophysics;1982-05
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