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At least 19 recordsLinked to original sources
PubMed1988

Structural and mixture analysis of glycerophosphoric acid derivatives by fast atom bombardment tandem mass spectrometry.

It is shown that by a combination of positive and negative FAB mass spectrometry with collision activation using a tandem mass spectrometer diacyl glycerophosphoric acid ester mixtures can be analysed. The following results will be obtained: Molecular masses of the single components, nature of the residue bound to the phosphoric acid (choline, serine etc.), fatty acids present in the single components and (if different) their location at C-1/C-2 as well as a quantitative analysis both of the fatty acids in the mixture and of the various species making up the latter.

Fatty Acids↗
PubMed1978

Streptococcus mutans dextransucrase: stimulation of glucan formation by phosphoglycerides.

Lysophosphatidylcholine (LPC) and other phosphoglycerides stimulated water-insoluble and water-soluble glucan production by the Streptococcus mutans 6715 dextransucrase (EC 2.4.1.5). LPC stimulated crude extracellular dextransucrase 1.7-fold, the water-insoluble glucan-producing alpha form of the enzyme 6.5-fold, the water-soluble glucan-producing beta form of the enzyme 2.1-fold, and the cell-associated dextransucrase 2.0-fold. Kinetic studies demonstrated that LPC did not change the K(m) for sucrose of alpha or beta but increased the maximum velocity of the enzymes. The K(m) for LPC of the alpha enzyme was 10(-5) M. LPC from various sources and synthetic preparations of lauroyl-LPC, myristoyl-LPC, and palmitoyl-LPC all stimulated glucan formation. Portions of phosphoglyceride molecules including fatty acids, phosphatidic acid, glycerophosphoric acid, glycerophos-phorylcholine, and choline, when tested individually or in combinations, did not enhance dextransucrase activity. The increased rates of glucan production caused by LPC and primer dextran were additive. Enzyme incubated with LPC before addition of sucrose was stimulated by dextran primer, and, conversely, enzyme treated with dextran was stimulated by addition of LPC with the sucrose substrate. Thus, dextransucrase can be activated by binding of intact phosphoglyceride molecules to a site on the enzyme that is distinct from either the glucosyl donor or glucosyl acceptor (primer) binding sites. Interactions between the S. mutans dextransucrase and amphipathic phosphoglycerides may explain properties of this enzyme which contribute to the cariogenicity of S. mutans.

Dextrans↗
PubMed1958

Pure phosphatides and the serodiagnosis of syphilis: relation of chemical structure to reactivity.

Several pure individual lecithins, all but one of which were synthetic, were used in cardiolipin antigens prepared for the VDRL microflocculation and Kolmer complement-fixation tests for syphilis.A number of compounds lacking one or more radicals of the lecithin molecule were used as substitutes for lecithin in an effort to determine reactive groupings.Several synthetic compounds related to cardiolipin, but simpler in structure, were tested as substitutes for it. Of these, certain fatty-acid derivatives of bis-(L-alpha-glyceryl)-phosphoric acid and of L-alpha-glycerophosphoric acid showed a limited reactivity in the VDRL and Kolmer tests.A number of weakly reactive antigens, in which both cardiolipin and lecithin had been replaced by synthetic compounds, were prepared for the VDRL test. The most reactive of these contained beta-(dioleoyl)-glycerophosphoric acid (sodium salt), dioleoyl lecithin and cholesterol.

Cholesterol↗