Interactions of pig plasma gelsolin with G-actin.
Pig plasma gelsolin forms a ternary complex with monomeric actin in 0.1 mM CaCl2 and a binary complex in EGTA (less than 0.01 microM calcium), as shown by gel filtration and fluorescence changes when actin which had been treated with N-ethylmaleimide and 7-chloro-4-nitrobenzeno-2-oxa-1,3-diazole (NBD-actin) or with N-(1-pyrenyl)iodoacetamide (PI-actin) binds to gelsolin. The fluorescence enhancement per actin molecule bound is similar in the binary and ternary complexes, but the affinity of gelsolin for labelled actin is very much greater in the presence of calcium. Furthermore, the formation of ternary complex exhibits strong positive cooperativity.
D000199:Actins / Q000097:blood*; D000345:Affinity Labels; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002118:Calcium / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000097:blood*; D002850:Chromatography, Gel; D018260:Gelsolin; D007201:Indicator Dilution Techniques; D008433:Mathematics; D008840:Microfilament Proteins / Q000097:blood*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013552:Swine
D000199:Actins; D000345:Affinity Labels; D002135:Calcium-Binding Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; D002118:Calcium