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The interaction between dansyl-labeled pollen calmodulin (D-pCaM) and synthesizedpeptides was studied in the presence of Ca2+ by fluorescence spectra. It is found that Gly/L- Ala→D-Ala substitution in peptide chains caused great changes in their affinity for pCaM. Besides.our data provided evidence on the dissimilarity of different CaMs although they haVe highlyconserved structures. A preliminary study was carried out on the effects of CaM-binding peptideson cellular signal transduction, cell proliferation, showing the participation of CaM in cellfunctions mentioned above.