17989-41-2Relevant articles and documents
Enzymic synthesis of sn-glycerol 3-phosphate.
Rios-Mercadillo,Whitesides
, p. 5828 (1979)
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Glycerol kinase: synthesis of dihydroxyacetone phosphate, sn-glycerol-3-phosphate, and chiral analogs.
Crans, Debbie C.,Whitesides, George M.
, p. 7019 - 7027 (1985)
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A toothpaste additive CGP new synthetic process of the (by machine translation)
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Paragraph 0041-0047, (2018/09/28)
The invention relates to a toothpaste additive new synthetic process of the CGP, specifically comprising the following steps: (1) under ice bath, is added to the glycerin in the POCl3 And catalyst, natural recovery to room temperature, stirring the reaction 5 - 6 h after, adds full and sodium bicarbonate solution adjusted to pH 8.0 - 9.0 after, adding calcium chloride, stirring at room temperature the reaction 10 - 12 hours, filter, collecting the filtrate; (2) to the step (1) of the filtrate obtained in adding anhydrous ethanol, stirring 0.5 - 1.0 h after, filtering, deposition and drying to obtain the CGP. (by machine translation)
Preparation method of L-alpha-glycerophosphoryl choline
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Paragraph 0041-0044; 0048, (2018/07/28)
The invention relates to a preparation method of L-alpha-glycerophosphoryl choline. The method comprises the steps of preparing (R)-3-chlorine-1,2-propylene glycol as an initial raw material; preparing (R)-glycerophosphate with calcium phosphate metal salt; then carrying out a reaction with dibromoethane to obtain (R)-3-glyceryl cyclophosphate; finally carrying out a reaction with trimethylamine in an open-loop reaction to obtain L-alpha-glycerophosphoryl choline. With the adoption of the method, the problem of wastewater pollution caused by choline chloride phosphate calcium salt or potassiumsalt is avoided, and the link of removing chloridion of a finished product through ion-exchange columns can be eliminated; the product purity is high; the yield is high; the method is applicable to industrial production and has a good application prospect.
The first nonradioactive fluorescence assay for phosphatidylglycerol: prolipoprotein diacylglyceryl transferase that initiates bacterial lipoprotein biosynthesis
Sundaram, Srividhya,Banerjee, Sanchari,Sankaran, Krishnan
scheme or table, p. 163 - 170 (2012/07/28)
The unique and physiologically vital bacterial enzyme, prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes the committed first step in the posttranslational transfer of diacylglyceryl group from phosphatidylglycerol to the prospective N-terminal cysteine of prolipoproteins, remains to be characterized for want of a simpler but equally sensitive nonradioactive assay. We, for the first time, report a coupled enzymatic fluorescence assay for Lgt using the de novo synthetic peptide substrate MKATKSAVGSTLAGCSSHHHHHH. The assay is based on the conversion of the by-product, glycerol-1-phosphate, to dihydroxyacetone using an alkaline phosphatase-glycerol dehydrogenase combination and estimating the fluorescence of the coupled reduction of resazurin to resorufin. The minimum amount of glycerol-1-phosphate, and hence the modified peptide, detected by this method is approximately 20 pmol, thereby making this assay a promising alternative to the radioactive assays. The assay is rapid, more convenient, less laborious, and suitable for purification and characterization of Lgt.
