英语翻译，很专业的生物英语，翻译器的不要，谢谢

Results:Membranefractionsfromthree-dayand200mMsalt-treatedArabidopsissuspensionplantswereisolated，followedbyproteaseshavingandenrichmentusingZirconiumion-chargedmagneticb... Results: Membrane fractions from three-day and 200 mM salt-treated Arabidopsis suspension plants were isolated， followed by protease shaving and enrichment using Zirconium ion-charged magnetic beads， and tandem mass spectrometry analyses. From this isolation， 18 phosphorylation sites from 15 Arabidopsis proteins were identified. A unique phosphorylation site in 14-3-3- interacting protein AHA1 was predominately identified in 200 mM salt-treated plants. We also identified some phosphorylation sites in aquaporins. A doubly phosphorylated peptide of PIP2;1 as well as a phosphopeptide containing a single phosphorylation site (Ser-283) and a phosphopeptide containing another site (Ser-286) of aquaporin PIP2;4 were identified respectively. These two sites appeared to be novel of which were not reported before. In addition， quantitative analyses of protein phosphorylation with either label-free or stable-isotope labeling were also employed in this study. The results indicated that level of phosphopeptides on five membrane proteins such as AHA1， STP1， Patellin-2， probable inactive receptor kinase (At3g02880)， and probable purine permease 18 showed at least two-fold increase in comparison to control in response to 200 mM salt-stress.