Photoaffinity modification of .DELTA.5-3-ketosteroid isomerase by light-activatable steroid ketones covalently coupled to agarose beads
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00279a035
Reference34 articles.
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4. Irreversible active-site-directed inhibition of Δ5-3-ketosteroid isomerase by steroidal 17-β-oxiranes. Evidence for two modes of binding in steroid-enzyme complexes
5. [43] Covalent affinity chromatography of penicillin-binding components from bacterial membranes
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1. Enzyme-catalyzed allylic rearrangements;Chemical Reviews;1990-11-01
2. Photoaffinity labeling of the oxysterol receptor.;Journal of Biological Chemistry;1988-02
3. Calcium release from calmodulin and its C-terminal or N-terminal halves in the presence of the calmodulin antagonists phenoxybenzamine and melittin measured by stopped-flow fluorescence with Quin 2 and intrinsic tyrosine. Inhibition of calmodulin-dependent protein kinase of cardiac sarcoplasmic reticulum;European Journal of Biochemistry;1986-09
4. Use of a solid-phase photoaffinity reagent to label a steroid binding site: application to the .DELTA.5-3-ketosteroid isomerase of Pseudomonas testosteroni;Biochemistry;1985-12
5. Modifications of ?5-3-ketosteroid isomerase induced by ultraviolet irradiation in the presence of the solid-phase photoaffinity reagent ?6-testosterone agarose;Journal of Protein Chemistry;1984-02
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