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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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Objective: This study sought to evaluate whether root dentine caries‐like lesions could be remineralised by saliva substitutes. Methods: Root dentine slabs (3 × 3 × 2 mm) were cut from bovine incisors, ground flat, polished and pre‐tested for Knoop microhardness (KHN) at five locations spaced 500 μm apart and 500 μm from the left edge of each sectioned piece. After 60 out of the 100 slabs had been selected based upon their KHN values, specimens were coated with wax except for their outer surface. Specimens were then cycled through a highly cariogenic challenge model to induce caries‐like lesions, whose formation was confirmed by KHN measurements located 500 μm from the right edge of the specimen. According to a randomised complete block design, the experimental units (n = 15) were exposed to 1.5 ml of saliva substitutes, based on either mucin (MC) or carboxymethylcellulose (CM), to natural human saliva (HS) or to 100% relative humidity (RH) over 20 days. Remineralisation was verified by KHN measurements located 1000 μm apart from the right edge of the specimen. Results: Analysis of variance indicated a significant (p < 0.0001) difference among the KHN values attained by the carious root dentine after exposure to the remineralising agents. Tukey's test ascertained that remineralisation was greatest with MC, intermediate with CM and least with HS, but rehardening did not reach the pre‐caries lesion formation values. Conclusion: Saliva substitutes may provide partial remineralisation to preformed caries‐like lesions in root dentine. 相似文献
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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.