Purification of oestrogen synthetase by high-performance liquid chromatography : Two membrane-bound enzymes from the human placenta
- 19 June 1985
- journal article
- Published by Elsevier in Journal of Chromatography A
- Vol. 326, 137-146
- https://doi.org/10.1016/s0021-9673(01)87439-2
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Fractionation of human red cell membrane proteins by ion-exchange chromatography in detergent on mono Q, with special reference to the glucose transporterJournal of Chromatography A, 1984
- Ion selectivity in the high-performance cation-exchange chromatography of proteinsJournal of Chromatography A, 1984
- Separation of proteins by high-performance anion-exchange chromatographyAnalytical Biochemistry, 1983
- Synthesis and properties of the epimeric 6-hydroperoxyandrostenediones, new substrates/inhibitors of human placental aromataseJournal of Steroid Biochemistry, 1983
- Purification of trypsin and other basic proteins by high-performance cation-exchange chromatographyJournal of Chromatography A, 1983
- Simple, efficient ternary solvent system for the separation of luteinizing hormone-releasing hormone and enkephalins by reversed-phase high-performance liquid chromatographyJournal of Chromatography A, 1983
- High-performance cation-exchange chromatography of proteinsAnalytical Biochemistry, 1983
- Recent Advances in HPLC Packings and ColumnsJournal of Chromatographic Science, 1980
- Studies on the microsomal mixed function oxidase system: redox properties of detergent-solubilized NADPH-cytochrome P-450 reductaseBiochemistry, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976