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PubMed2006

Synthesis of Staphylococcus aureus lipoteichoic acid derivatives for determining the minimal structural requirements for cytokine induction.

For the investigation of the minimal structural requirements for cytokine induction, Staphylococcus aureus lipoteichoic acid derivatives with two, three, four, and five glycerophosphate backbone moieties, carrying each a d-alanyl residue, were needed. Based on two different glycerophosphate building blocks and 6b-O-phosphitylated gentiobiosyl diacylglycerol the desired target molecules (compounds 1-4) could be readily obtained and provided for biological studies.

Cytokines↗

PubMed1988

Glucose flux and the redox state of pyridine dinucleotides in the rat lens.

The concentration of alpha-glycerophosphate (GP) appeared to increase and readily reached a new steady state in lenses incubated with KCN or under hyperglucosic condition. This increase can be explained by the change in NADH/NAD ratio under each condition. The relative ratio of pyridine dinucleotides (NADH/NAD) was calculated from equilibrium equations of two NAD-linked enzymes, lactate dehydrogenase (LDH) and alpha-glycerophosphate dehydrogenase (GPDH). The change in NADH/NAD ratio based on biochemical assays correlates well with that estimated from GPDH reaction. This indicates that measurements of pyridine dinucleotides (e.g. in vivo redox fluorometry) can be used to demonstrate lens metabolic status.

Animals↗

PubMed1985

The function of redox shuttles during aerobic glycolysis in two strains of Ehrlich ascites tumor cells.

The function of glycerophosphate and malate-aspartate shuttles during glucose metabolism in two strains of Ehrlich ascites tumor cells was evaluated by several experimental approaches. The activities of the enzymes involved in these shuttle systems were assayed in the cytosolic and mitochondrial compartments after cell fractionation by the digitonin method. The glycerophosphate shuttle can be ruled out because of the lack of relevant enzymatic activities, and the failure of glucose to increase rotenone-inhibited respiration. Analysis of glycolytic flux in the presence of aminooxyacetate indicates that the activity of malate-aspartate shuttle may be very low. Balance studies of glucose uptake and lactate production suggest the existence of other pathways for the reoxidation of cytosolic NADH, which are acetyl-CoA dependent. Estimation of citrate synthase and ATP citrate lyase, in addition to the observed high activity of malate dehydrogenase, suggests a malate-citrate shuttle.

Aerobiosis↗

PubMed2000

Glucosylcaldarchaetidylglycerol, a minor phosphoglycolipid from Thermoplasma acidophilum.

A novel phosphoglycolipid (GPL-K) was isolated from Thermoplasma acidophilum (ATCC 27658). The chemical components of GPL-K were analyzed by gas liquid chromatography and GC-MS. The sugar moiety of GPL-K and its anomeric region were analyzed by NMR assignment. The core lipid of GPL-K was caldarchaeol, and its main hydrocarbon chains were acyclic and monocyclic C(40) biphytanyl. The polar head groups were alpha-glucose and glycerophosphate. The negative FAB-MS spectrum of GPL-K confirmed that the lipid peak of m/z 1614 consists of a caldarchaeol (including one cyclopentane ring), a hexose sugar, and a glycerophosphate. We have proposed the tentative structure of GPL-K.

Carbohydrate Sequence↗

PubMed2000

Ecto-alkaline phosphatase in NG108-15 cells : a key enzyme mediating P1 antagonist-sensitive ATP response.

We previously demonstrated that extracellular adenine nucleotides induced cyclic AMP elevation through local adenosine production at the membrane surface and subsequent activation of adenosine A(2A) receptors in NG108-15 cells. Furthermore, the adenosine formation was found to be mediated by an ecto-enzyme distinct from the ecto-5'-nucleotidase (CD73). In this study, we investigated the properties of the ecto-AMP phosphohydrolase activity in NG108-15 cells. NG108-15 cells hydrolyzed AMP to adenosine with the K:(M:) value of 18.8+/-2.2 microM and V(max) of 5.3+/-1.6 nmol min(-1) 10(6) cells(-1). This activity was suppressed at pH 6.5, but markedly increased at pH 8.5. The AMP hydrolysis was blocked by levamisole, an alkaline phosphatase (ALP) inhibitor. NG108-15 cells released orthophosphate from 2'- and 3'-AMP as well as from ribose-5-phosphate and ss-glycerophosphate, indicating that NG108-15 cells express ecto-ALP. The cyclic AMP accumulation induced by several adenine nucleotides was inhibited by levamisole, p-nitrophenylphosphate and ss-glycerophosphate, with a parallel decrease in the extracellular adenosine formation. Reverse transcriptase polymerase chain reaction analysis revealed that NG108-15 cells express mRNA for the tissue-nonspecific isozyme of ALP. These results demonstrate that AMP phosphohydrolase activity in NG108-15 cells is due to ecto-ALP, and suggest that this enzyme plays an essential role for the P1 antagonist-sensitive ATP-induced cyclic AMP accumulation in NG108-15 cells.

Adenosine↗

PubMed1965

The metabolism of glucose by the rabbit lens in the presence and absence of oxygen.

1. The effect of the absence of oxygen on the metabolism of [U-(14)C]glucose by the rabbit lens has been examined. 2. Protein-free extracts of incubated lens were subjected to electrophoresis followed by chromatography on paper; radioautographs showed 10 compounds substantially labelled. In the absence of oxygen, less radioactivity appeared in glucose, sorbitol, fructose, alanine, glutamic acid, glutathione and nucleotides, and more in lactic acid, alpha-glycerophosphate and glycerol. 3. The radioactivity of lens protein was about two to four times greater after aerobic than after anaerobic incubation. 4. The radioactivity of carbon dioxide was 2- to 4-fold greater after aerobic incubation than after anaerobic incubation. 5. After aerobic incubation of the lens, the radioactivity of all the labelled compounds was higher in the outer part (cortex) than in the inner part (nucleus). 6. Free glycerol has been found to be present in the lens. Its concentration, and that of alpha-glycerophosphate, has been measured in the lens of several species of animal.

Alanine↗

PubMed1967

The chemical nature of the products obtained by the action of cabbage-leaf phospholipase D on lysolecithin: the structure of lysolecithin.

1. Lysolecithin, prepared by the action of snake-venom phospholipase A on ovolecithin, when incubated with Savoy-cabbage phospholipase D, in the presence of Ca(2+) ions, gave two degradation products (designated A and B) in the form of their calcium salts. 2. These calcium salts were separated quantitatively by solvent fractionation and converted into the corresponding sodium salts. 3. Substance B proved to be a lysophosphatidic acid of conventional structure (1-monoacyl-l-3-glycerophosphoric acid). When the phosphate group was removed by means of prostatic acid phosphomonoesterase, a 1-monoglyceride was formed quantitatively. Alkaline hydrolysis gave the theoretical yield of l-3-glycerophosphate. 4. Substance A, on the other hand, had all the properties expected for a cyclic phosphate of a 1-monoglyceride. It was unaffected by phosphomonoesterase. On alkaline hydrolysis, the acyl group was removed and ring opening of the presumed cyclic phosphate group gave an approximately equimolar mixture of 2- and l-3-glycerophosphates. 5. The structures of substances A and B confirm lysolecithin as 1-monoacyl-l-3-glycerylphosphorylcholine.

Acid Phosphatase↗

PubMed1967

Studies on alkaline phosphatase. Inhibition by phosphate derivatives and the substrate specificity.

1. The kinetics of inhibition of calf-intestinal alkaline phosphatase by inorganic phosphate, fluorophosphate, inorganic pyrophosphate, beta-glycerophosphate and adenosine 5'-triphosphate in the range pH8-10 were investigated. The reference substrate was 4-methylumbelliferyl phosphate. 2. The inhibitions were ;mixed' in that both K(m) and V were affected, but the competitive element was by far the stronger. 3. In each case the pH profile for the competitive K(i) was similar to the pH profile for K(m). Since the K(m) and K(i) values both change 100-fold over the pH range 8-10, it is concluded that the inhibitors compete with the substrate for the same active site. 4. It was also found that the enzyme preparation hydrolysed fluorophosphate, pyrophosphate and adenosine 5'-triphosphate as readily as it hydrolysed 4-methylumbelliferyl phosphate and beta-glycerophosphate. Each pH-activity curve, however, had a different shape, but with the exception of pyrophosphate the activity approached the same maximum value at high pH. 5. Attempts to separate the phosphomonoesterase and pyrophosphatase activities by column chromatography were not successful, and the results of other experiments listed suggest that the two activities are a property of the same enzyme. 6. The effect of Mg(2+) ions is briefly mentioned: the phosphomonoesterase activity is enhanced whereas the pyrophosphatase and adenosine triphosphatase activities are strongly inhibited in the presence of excess of Mg(2+) ions.

Alkaline Phosphatase↗

PubMed1968

Factors affecting the glucose 6-phosphate inhibition of hexokinase from cerebral cortex tissue of the guinea pig.

1. The inhibition of hexokinase by glucose 6-phosphate has been investigated in crude homogenates of guinea-pig cerebral cortex by using a sensitive radio-chemical technique for the assay of hexokinase activity. 2. It was observed that 44% of cerebral-cortex hexokinase activity did not sediment with the microsomal or mitochondrial fractions (particulate fraction), and this is termed soluble hexokinase. The sensitivities of soluble and particulate hexokinase, and hexokinase in crude homogenates, to the inhibitory actions of glucose 6-phosphate were measured; 50% inhibition was produced by 0.023, 0.046 and 0.068mm-glucose 6-phosphate for soluble, particulate and crude homogenates respectively. 3. The optimum Mg(2+) concentration for the enzyme was about 10mm, and this appeared to be independent of the ATP concentration. In the presence of added glucose 6-phosphate, raising the Mg(2+) concentration to 5mm increased the activity of hexokinase, but above this concentration Mg(2+) potentiated the glucose 6-phosphate inhibition. When present at a concentration above 1mm, Ca(2+) ions inhibited the enzyme in the presence or absence of glucose 6-phosphate. 4. When the ATP/Mg(2+) ratio was 1.0 or below, variations in the ATP concentration had no effect on the glucose 6-phosphate inhibition; above this value ATP inhibited hexokinase in the presence of glucose 6-phosphate. ATP had an inhibitory effect on soluble hexokinase similar to that on a whole-homogenate hexokinase, so that the ATP inhibition could not be explained by a conversion of particulate into soluble hexokinase (which is more sensitive to inhibition by glucose 6-phosphate). It is concluded that ATP potentiates glucose 6-phosphate inhibition of cerebral-cortex hexokinase, whereas the ATP-Mg(2+) complex has no effect. Inorganic phosphate and l-alpha-glycerophosphate relieved glucose 6-phosphate inhibition of hexokinase; these effects could not be explained by changes in the concentration of glucose 6-phosphate during the assay. 5. The inhibition of hexokinase by ADP appeared to be independent of the glucose 6-phosphate effect and was not relieved by inorganic phosphate. 6. The physiological significance of the ATP, inorganic phosphate and alpha-glycerophosphate effects is discussed in relation to the control of glycolysis in cerebral-cortex tissue.

Adenine Nucleotides↗

PubMed1974

Energy-linked reduction of nicotinamide--adenine dinucleotide in membranes derived from normal and various respiratory-deficient mutant strains of Escherichia coli K12.

1. Assay conditions are described for the ATP-dependent, uncoupler-sensitive, energy-linked reduction of NAD(+) by succinate, dl-alpha-glycerophosphate or d-lactate in membranes from aerobically grown Escherichia coli. 2. The reaction may be demonstrated in electron-transport particles (ET particles) from cells grown in glycerol, but not in depleted particles washed in low-ionic-strength buffer, or in ET particles from cells grown in glucose. 3. The latter two classes of particles have low specific activities of ATPase (adenosine triphosphatase), succinate dehydrogenase, dl-alpha-glycerophosphate dehydrogenase and d-lactate dehydrogenase relative to undepleted ET particles from cells grown in glycerol. 4. Reconstitution of energy-linked NAD(+) reduction in particles from cells grown in glucose was done by: (a) addition of the high-speed supernatant fraction from sonicates of the same cells; (b) addition of a protein fraction, precipitated by (NH(4))(2)SO(4) from this supernatant, or (c) addition of an (NH(4))(2)SO(4)-precipitated fraction from the low-ionic-strength wash of particles from cells grown in glycerol. 5. The use of (NH(4))(2)SO(4)-precipitated fractions from ATPase- or succinate dehydrogenase-deficient mutants grown in glycerol in the above reconstitution indicated that failure to demonstrate the reaction in particles from cells grown in glucose was a result of inadequate activities of appropriate dehydrogenases, rather than of ATPase. 6. Energy-linked NAD(+) reduction could be demonstrated in particles from a ubiquinone-deficient mutant only after restoration of NADH oxidase activity by adding ubiquinone-1. 7. The measured rate of the energy-linked reaction in particles from a haem-deficient mutant, however, was not stimulated after the ATP- and haematin-dependent acquisition of functional cytochromes. 8. Results are interpreted as evidence of the ubiquinone-dependent, but cytochrome-independent, nature of the site I region of the respiratory chain in E. coli.

Adenosine Triphosphatases↗

PubMed1981

Regulation of hepatic fatty acid metabolism. The activities of mitochondrial and microsomal acyl-CoA:sn-glycerol 3-phosphate O-acyltransferase and the concentrations of malonyl-CoA, non-esterified and esterified carnitine, glycerol 3-phosphate, ketone bodies and long-chain acyl-CoA esters in livers of fed or starved pregnant, lactating and weaned rats.

1. The concentrations of malonyl-CoA, glycerol 3-phosphate, non-esterified carnitine, acid-soluble and acid-insoluble acylcarnitines, acetoacetate, 3-hydroxybutyrate and acid-insoluble acyl-CoA were measured in rapidly-frozen liver samples from fed or starved (24h) virgin, pregnant (19-20 days), lactating (2, 10-12 and 18-20 days) and weaned (for 24h, on 10th day of lactation) rats. The activities of total and N-ethylmaleimide-sensitive and -insensitive glycerophosphate acyltransferase (acyl-CoA:sn-glycerol 3-phosphate O-acyltransferase; EC 2.3.1.15) were also measured. 2. The concentration of malonyl-CoA was significantly higher in liver of fed pregnant, mid- and late-lactating rats than in liver of fed virgin rats. After starvation for 24h hepatic malonyl-CoA concentrations were higher in mid-lactating rats and lower in pregnant and weaned rats than in virgin animals. 3. After starvation for 24h the hepatic concentrations of glycerol 3-phosphate, ketone bodies, acid-soluble acylcarnitines and the value for the [3-hydroxybutyrate]/[acetoacetate] ratio were all highest in pregnant rats, intermediate in virgin, 2-day lactating and weaned animals and lowest in mid- and late-lactating rats. The concentrations of acid-insoluble acylcarnitines also increased most in pregnant rats, after starvation. The concentration of acid-insoluble acyl-CoA increased equally after starvation in virgin and pregnant animals but did not increase significantly in all other animals studied. 4. The total concentration of carnitine was similar in livers of fed virgin, pregnant and 2-day lactating animals but fell markedly by the 10th day of lactation and remained low in late-lactating animals. The concentration of non-esterified carnitine followed the same pattern. After starvation for 24h the hepatic concentration of non-esterified carnitine decreased significantly in virgin, pregnant and 2-day lactating animals, but remained unchanged in mid- and late-lactating or weaned animals. 5. The activities of N-ethylmaleimide-sensitive and -insensitive glycerophosphate acyltransferase both increased significantly in livers of mid-lactating animals. After starvation for 24h the activity of the N-ethylmaleimide-insensitive O-acyltransferase decreased in livers of virgin, pregnant and mid-lactating animals, whereas the activity of the N-ethylmaleimide-sensitive O-acyltransferase was unchanged in virgin animals but decreased markedly in livers of pregnant and lactating rats. 6. The results are discussed in relation to the importance of different metabolic parameters in the regulation of long-chain acyl-CoA metabolism in the liver.

Acyl Coenzyme A↗

PubMed1973

Metabolism of membrane phospholipids and its relation to a novel class of oligosaccharides in Escherichia coli.

Phosphatidylethanolamine is metabolically stable in exponentially growing cells of Escherichia coli, whereas phosphatidylglycerol and cardiolipin (diphosphatidylglycerol), labeled by growth in the presence of sn-[2-(3)H]glycero-3-(32)P, lose their radioactivity during subsequent growth on unlabeled medium. We have found that the loss of label from the lipid fraction is accompanied by its appearance in a novel type of cell constituent of E. coli, a closely related group of oligosaccharides, each containing glycerol and phosphoric acid in equimolar proportions, probably derived as intact glycerophosphate units from phosphatidylglycerol and/or cardiolipin. Glucose is the sole detectable sugar. The glycerophosphate-containing oligosaccharides may be fractionated by ion-exchange chromatography into several subfractions, some of which contain succinic acid in ester linkage. Although apparently derived from membrane phospholipids, the newly discovered substances contain no fatty acids, are soluble in water, and are insoluble in organic solvents such as chloroform. They comprise about 0.5-1% of the dry weight of growing cells.

Cardiolipins↗

PubMed1975

Isolation of Escherichia coli mutants defective in enzymes of membrane lipid synthesis.

A new method has been developed which permits the rapid screening of E. coli colonies for mutants with defective enzymes of phospholipid metabolism. In this procedure, a disc of filter paper is pressed down on an agar plate containing several hundred colonies of mutagen-treated cells, after which the paper is lifted off. In the process the colonies are transferred to the paper, giving rise to a replica print of the master plate. The few cells from each colony left on the master keep growing in the original pattern. The pattern of colonies is also retained on the filter paper, even after the cells are rendered permeable with lysozyme and EDTA. Colonies treated in this manner remain absorbed to the paper, where they can convert sn-(U-14-C)glycero-3-P to phosphatidyl(U-14-C)glycerophosphate, dependent on added CDP-diglyceride. Unrelated reactions of sn-(U-14-C)glycero-3-P that may obscure the synthesis of phosphatidyl-glycerophosphate are inhibited by the addition of reagents poisoning energy generation. The radioactive phospholipid that forms around each colony on the paper is precipitated in situ with trichloroacetic acid, and unreacted sn-(U-14-C)glycero-3-P is washed away. After autoradiography, the colonies on the filter paper are stained with Coomassie blue. When the autoradiogram is superimposed on the strained paper, mutants are identified as blue colonies lacking a black halo. With this method, 20,000 colonies were screened in several days. Four mutants were identified with low levels of CDP-diglyceride:snglycero-3-P phosphatidyl transferase (EC 2.7.8.5, GLYCEROL-PHOSPHATE PHOSPHATIDYLTRANSFERASE, PHOSPHATIDYLGLYCEROPHOSPHATE SYNTHETASE) IN EXTRACTS. With a similar assay, 10,000 additional colonies were screened for mutants with altered CDP-diglyceride:L-serine O-phosphatidyltransferase (EC 2.7.8.8, phosphatidylserine synthetase), and four strains were found in which the enzyme is thermolabile. The screening technique described here is termed replica printing and should be applicable not only to studies of phospholipid metabolism but also to nucleic acid and protein synthesis.

Autoradiography↗

PubMed2002

Two- versus three-dimensional in vitro differentiation of human pulp cells into odontoblastic cells.

The spatial organization of the pulp cells may modify the cytodifferentiation process. The purpose of this study was to compare the two- versus three-dimensional cell culture systems for differentiation of human odontoblastic cells in vitro. Pulpal cores from freshly extracted human third molars were cultured in vitro in a perfusion device on two types of membranes: polyester membrane (two-dimensional [2D] cell culture) and nylon mesh (three-dimensional [3D] cell culture). The cells were incubated with minimum essential medium containing (a) substitute serum, (b) 10% fetal calf serum (FCS), (c) 10% fetal calf serum + 2 mM beta-glycerophosphate (beta GP), and (d) 10% fetal calf serum + transforming growth factor (TGF) beta 1. Immunohistochemistry was used to evaluate the expression of collagen I, osteonectin, and nestin. Small differences were observed between 2D and 3D cell culture systems. This was particularly evident in the 10% FCS group. beta-Glycerophosphate in the 3D system seems to stimulate the osteogenic cell phenotype, as a considerable induction of osteonectin is observed.

Adolescent↗

PubMed2001

Differentiation of osteoblasts and in vitro bone formation from murine embryonic stem cells.

Pluripotent embryonic stem (ES) cells have the potential to differentiate to all fetal and adult cell types and might represent a useful cell source for tissue engineering and repair. Here we show that differentiation of ES cells toward the osteoblast lineage can be enhanced by supplementing serum-containing media with ascorbic acid, beta-glycerophosphate, and/or dexamethasone/retinoic acid or by co-culture with fetal murine osteoblasts. ES cell differentiation into osteoblasts was characterized by the formation of discrete mineralized bone nodules that consisted of 50-100 cells within an extracellular matrix of collagen-1 and osteocalcin. Dexamethasone in combination with ascorbic acid and beta-glycerophosphate induced the greatest number of bone nodules and was dependent on time of stimulation with a sevenfold increase when added to ES cultures after, but not before, 14 days. Co-culture with fetal osteoblasts also provided a potent stimulus for osteogenic differentiation inducing a fivefold increase in nodule number relative to ES cells cultured alone. These data demonstrate the application of a quantitative assay for the derivation of osteoblast lineage progenitors from pluripotent ES cells. This could be applied to obtain purified osteoblasts to analyze mechanisms of osteogenesis and for use of ES cells in skeletal tissue repair.

Animals↗

PubMed1997

Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic beta-cells.

In the pancreatic beta-cell, insulin secretion is stimulated by glucose metabolism resulting in membrane potential-dependent elevation of cytosolic Ca2+ ([Ca2+]c). This cascade involves the mitochondrial membrane potential (delta psi[m]) hyperpolarization and elevation of mitochondrial Ca2+ ([Ca2+]m) which activates the Ca(2+)-sensitive NADH-generating dehydrogenases. Metabolism-secretion coupling requires unidentified signals, other than [Ca2+]c, possibly generated by the mitochondria through the rise in [Ca2+]m. To test this paradigm, we have established an alpha-toxin permeabilized cell preparation permitting the simultaneous monitoring of [Ca2+] with mitochondrially targeted aequorin and insulin secretion under conditions of saturating [ATP] (10 mM) and of clamped [Ca2+]c at substimulatory levels (500 nM). The tricarboxylic acid (TCA) cycle intermediate succinate hyperpolarized delta psi(m), raised [Ca2+]m up to 1.5 microM and stimulated insulin secretion 20-fold, without changing [Ca2+]c. Blockade of the uniporter-mediated Ca2+ influx into the mitochondria abolished the secretory response. Moreover, glycerophosphate, which raises [Ca2+]m by hyperpolarizing delta psi(m) without supplying carbons to the TCA cycle, failed to stimulate exocytosis. Activation of the TCA cycle with citrate evoked secretion only when combined with glycerophosphate. Thus, mitochondrially driven insulin secretion at permissive [Ca2+]c requires both a substrate for the TCA cycle and a rise in [Ca2+]m. Therefore, mitochondrial metabolism generates factors distinct from Ca2+ and ATP capable of inducing insulin exocytosis.

Adenosine Triphosphate↗

PubMed1986

Diet effects on membrane phospholipid fatty acids and mitochondrial function in BHE rats.

The effects of feeding a 5% corn oil or coconut oil diet on the composition of hepatic phospholipid fatty acids and on hepatic mitochondrial function were studied. Male BHE weanling rats were fed a 65% starch diet containing 5% corn or coconut oil. Rats were decapitated, and hepatic tissue was used for phospholipid fatty acid analysis and for the preparation of mitochondria. Mitochondrial ATPase activity, alpha-glycerophosphate and malate-aspartate shuttle activity, and succinate- or pyruvate-supported respiration were determined. Livers from rats fed the coconut oil diet had more saturated phospholipid fatty acids than those from rats fed the corn oil diet. ATPase activity and the activity of the malate-aspartate shuttle were not affected by diet. The activity of the alpha-glycerophosphate shuttle was greater in rats fed the coconut oil diet than in rats fed the corn oil diet. Succinate-supported state 3 respiration was not affected by diet, whereas succinate-supported state 4 respiration was higher in mitochondria from rats fed coconut oil than in rats fed corn oil. Evidence of uncoupling of pyruvate-supported respiration from ATP synthesis was observed in mitochondria from rats fed coconut oil but not in rats fed corn oil. These observations suggest that the inherent tendency of the BHE rat toward looser coupling of respiration to ATP synthesis is potentiated by the feeding of the highly saturated fat, hydrogenated coconut oil.

Adenosine Diphosphate↗

PubMed1987

'Lipoteichoic acid' of Bifidobacterium bifidum subspecies pennsylvanicum DSM 20239. A lipoglycan with monoglycerophosphate side chains.

The lipid macroamphiphile of Bifidobacterium bifidum subsp. pennsylvanicum DSM 20239 was extracted with phenol/water and purified by treatment with nucleases and hydrophobic interaction chromatography. From analytical data, the results of Smith degradation, hydrolysis with HF and methylation studies, the following structure is proposed: (formula; see text) where n and m are approximately 7-10 and 8-15, respectively. The monoglycerophosphate residues have the sn-glycero-1-phosphate configuration; 20-50% of them are substituted with L-alanine in ester linkage. The lipid anchor is most likely a galactosyldiacylglycerol, part of which carries a third fatty acid. This is the first example among gram-positive bacteria of a glycerophosphate-containing lipid macroamphiphile that carries the glycerophosphate residues as monomeric side chains on a lipoglycan. Further, it contains L-alanine in place of the D-alanine found in lipoteichoic acids.

Bifidobacterium↗