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1.
Use of the pressure vessel to measure concentrations of solutes in apoplastic and membrane-filtered symplastic sap in sunflower leaves 总被引:7,自引:0,他引:7
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A simple, repeatable, and accurate method is described for the collection of apoplastic and membrane-filtered symplastic sap fractions, and for the determination of the origin of these fractions within the leaf. The apoplastic distribution patterns of the naturally occurring apoplastic leaf solutes, and the apoplastic dye PTS (trisodium 3-hydroxy-5, 8, 10-pyrenetrisulfonate) were compared. Aliquots of sap were expressed from detached sunflower leaves in a pressure chamber over intervals of 0.02 to 0.04 megapascal. Three distinct fractions were detected in the expressed sap volume. These were successively released and identified as a petiole-midrib fraction, a minor vein-cell wall fraction, and a mixed fraction consisting of a contribution from the minor vein-cell wall with an increasing proportion of membrane-filtered cell sap. 相似文献
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C Crone J Frokjaer-Jensen JJ Friedman O Christensen 《The Journal of general physiology》1978,71(2):195-220
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Lipoteichoic acid is an important microbe-associated molecular pattern of Lactobacillus rhamnosus GG
Claes Ingmar JJ Segers Marijke E Verhoeven Tine LA Dusselier Michiel Sels Bert F De Keersmaecker Sigrid CJ Vanderleyden Jos Lebeer Sarah 《Microbial cell factories》2012,11(1):1-8
Background
Receptors with a single transmembrane (TM) domain are essential for the signal transduction across the cell membrane. NMR spectroscopy is a powerful tool to study structure of the single TM domain. The expression and purification of a TM domain in Escherichia coli (E.coli) is challenging due to its small molecular weight. Although ketosteroid isomerase (KSI) is a commonly used affinity tag for expression and purification of short peptides, KSI tag needs to be removed with the toxic reagent cyanogen bromide (CNBr).Result
The purification of the TM domain of p75 neurotrophin receptor using a KSI tag with the introduction of a thrombin cleavage site is described herein. The recombinant fusion protein was refolded into micelles and was cleaved with thrombin. Studies showed that purified protein could be used for structural study using NMR spectroscopy.Conclusions
These results provide another strategy for obtaining a single TM domain for structural studies without using toxic chemical digestion or acid to remove the fusion tag. The purified TM domain of p75 neurotrophin receptor will be useful for structural studies. 相似文献10.