ArticleThe Biochemical journal1993
The interaction of 6-propionyl-2-(NN-dimethyl)aminonaphthalene (PRODAN)-labelled actin with actin-binding proteins and drugs.
Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 15 citations in OpenAlex.
- Biomolecular mimicry in the actin cytoskeleton: mechanisms underlying the cytotoxicity of kabiramide C and related macrolides.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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1 author at 1 institution in 1 country.
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Abstract
The influence of various actin-binding proteins and drugs on the fluorescence emission of rabbit muscle actin labelled with the fluorescent probe acrylodan (6-acryloyl-2-dimethylaminonaphthalene) at Cys-374, the penultimate amino acid residue of the actin amino acid sequence, was studied. Addition of myosin, tropomyosin or phalloidin, agents known to bind only to filamentous F-actin, did not change the emission energy or the integrated intensity of the fluorescence spectrum. The presence of heavy meromyosin or of the glycolytic enzyme aldolase led to a small (approx. 2%) increase in the integrated intensity, and in the energy of the emitted fluorescence. The interaction of 6-propionyl-2-(NN-dimethyl)aminonaphthalene (PRODAN)-F-actin with pancreatic DNAase I and with a filament-severing 19 kDa protein from pig brain resulted in the gradual reduction of the integrated intensity of the emission and a red shift of the emission energy, suggestive of a disintegration of the actin filament structure. Profilin caused a < 10% change in the emission energy. Cytochalasin D reduced the integrated intensity of PRODAN-F-actin and red-shifted the emission energy, while cytochalasin B was without influence. Pancreatic DNAase I did not change the fluorescence emission of PRODAN-G-actin, suggesting that binding of this enzyme does not alter the environment of the probe. When the 19 kDa protein bound to PRODAN-G-actin, however, the integrated intensity was reduced and the emission energy was lowered. This effect was exploited to estimate the binding constant for the interaction between the 19 kDa protein and PRODAN-G-actin. The Kd was found to be about 0.25 microM.
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