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PubMed1976

Zonal rotor analysis of the subcellular localization of alpha-glycerphosphate dehydrogenase, alpha-naphthyl palmitate and beta-naphthyl laurate hydrolases in the mucosa of the guinea-pig small intestine.

Whole homogenate of guinea-pig small intestine mucosa was analysed by centrifugation in a zonal rotor. The results indicate that FAD-linked alpha-glycerophosphate dehydrogenase is localized in the mitochondria and that NAD-linked alpha-glycerophosphate dehydrogeanse is a soluble phase enzyme. An enzyme hydrolysing alpha-naphthyl palmitate at an acid pH was localized in the lysosomes and was activated by 0.1% Triton X-100 and by freezing and thawing. An alkaline hydrolase acting on beta-naphthyl laurate was localized in the 'microsomes'. The possibility of this enzyme being different from alpha-naphthyl acetate hydrolase is discussed.

Animals↗

PubMed1991

Lectin binding in skeletal muscle. Evaluation of alkaline phosphatase conjugated avidin staining procedures.

Cryostat sections from rat gracilis muscles were incubated with different biotinylated lectins: Con A (Concanavilin A), WGA (Wheat germ agglutinin), SBA (soybean agglutinin), GS I and GS II (Griffonia simplicifolia agglutinin), LCA (Lens culinaris agglutinin), PNA (peanut agglutinin) and PSA (Pisum sativum agglutinin). The sections were subsequently treated with alkaline phosphatase conjugated avidin. The lectin binding sites were visualized after incubation in substrate media containing: (1) 5-bromo-4-chloro indoxyl phosphate and Nitro Blue tetrazolium or copper sulphate; (2) naphthol AS-MX phosphate or naphthol AS-BI phosphate and various types of diazonium salts; (3) alpha-naphthylphosphate and Fast Blue BB; (4) beta-glycerophosphate according to the method of Gomori. The results obtained with the alkaline phosphatase methods were compared with those seen with a streptavidin-horseradish peroxidase procedure. Several chromogen protocols for visualizing alkaline phosphatase activity showed differences in the ability to detect lectin binding sites. A sarcoplasmic reaction was evident for Con A, GS II, WGA, LCA, and PSA after incubation in the indoxyl phosphate medium. Sarcoplasmic reaction for GS II was also noticed after incubation with naphthol AS-MX Fast Blue BB and beta-glycerophosphate. The latter substrate also gave rise to a sarcoplasmic Con A reaction. With the indoxylphosphate tetrazolium salt method some muscle fibres showed a very strong intracellular reaction after incubation with Con A and GS II while the staining intensity was weak in other fibres. The same muscle fibres were stained with PAS. No sarcoplasmic reactions were observed with either naphthol phosphate media or with the diaminobenzidine peroxidase methods. Further, the staining of the muscle fibre periphery, connective tissue, an capillaries was intensified using the indoxyl method. The indoxylphosphate-tetrazolium salt method seems to be suitable for future investigations of lectin binding sites in muscle sections.

Alkaline Phosphatase↗

PubMed1978

Cyanamide mediated syntheses under plausible primitive earth conditions. V. The synthesis of phosphatidic acids.

A mixture of ammonium palmitate, 14C-sn-glycero-1(3)-phosphate, cyanimide and imidazole when heated for several hours formed significant quantities of phospholipids. These reaction products were shown by chromatographic, chemical and enzymatic procedures to be monopalmitoylglycerophosphate (MPGP), dipalmitoylglycerophosphate (DPGP) and monopalmitoyl cyclic glycerophosphate (cMPGP). A portion of the MPGP and DPGP possessed the same steric configuration as naturally occurring lysophosphatidic acid and phosphatidic acid. The yield of total phospholipid was maximal at temperatures between 60 degrees and 90 degrees after 8 h. When ratios of reactants were varied, up to 45% of radioactive glycerophosphate was converted into phospholipids. The average proportions of individual phosphatidic acids were: 60% MPGP, 27% DPGP and 13% cMPGP. Evidence was obtained for a synergistic relationship between cyanamide and imidazole in promoting the formation of phosphatidic acids. These results suggest that phosphatidic acids, which are essential precursors for the biochemical synthesis of more complex membrane phospholipids, could have been produced on the primitive Earth.

Cyanamide↗

PubMed1996

In situ determination of different dehydrogenase activity profiles in the linings of odontogenic keratocysts and radicular cysts.

The levels of succinate, lactate, glutamate, glycerophosphate and glucose-6-phosphate dehydrogenases within the linings of keratinizing and non-keratinizing odontogenic cysts were investigated using static end-point and continuously monitored Nitroblue Tetrazolium-based histochemical methods. The use of TV image analysis for quantification of formazan final reaction products was validated by demonstrating significant relationships between the integrated absorbance at 585 nm and the amount of formazan in, and thickness of, gelatin films containing reduced tetrazolium salt (r = 1.0, p < 0.001). Absorbance readings of stained sections gave mean coefficients of variation of 1.8 +/- 0.9% between day of measurement, and of 5.65 +/- 1.32% between serial sections. End-point assays indicated that the linings of odontogenic keratocysts contained higher levels of glucose-6-phosphate dehydrogenases (p < 0.0002) and lower levels of lactate dehydrogenase (p < 0.002) than those of radicular cysts. Succinate, glutamate and glycerophosphate dehydrogenase activities were similar in both cyst types. Results from continuously monitored assays, performed for glucose-6-phosphate and succinate dehydrogenases, demonstrated linear reaction rates over the first 2.75 min of reaction. The calculated enzyme activities from continuous assays were between 1.49 and 3.49 times higher than those determined from end-point assays and confirmed that levels of glucose-6-phosphate dehydrogenase were significantly higher in the linings of odontogenic keratocysts than those of radicular cysts (p < 0.004). By contrast, succinate dehydrogenase activity was significantly higher in radicular cyst linings (p < 0.03). These results highlight the benefits of an approach to in situ determination of enzyme activity using image analysis and continuous monitoring methodologies. Overall, the high level of glucose-6-phosphate dehydrogenase found in keratocyst linings is consistent with their clinical behaviour and higher level of proliferation and synthetic activity whereas the level of lactate dehydrogenase in radicular cysts probably reflects the presence of local tissue damage within these inflammatory lesions.

Histocytochemistry↗

PubMed1978

Esterification of palmitic acid in swine aortic homogenates.

The incorporation of [1-14C] palmitic acid into tissue lipids of the medial and intimal layers of swine aortic homogenates was investigated. The homogenates obtained were metabolically active as indicated by their ready incorporation of labeled palmitic acid into phospholipids, diglycerides and triglycerides in the presence of alpha-glycerophosphate in the incubation medium. Predominantly, labeling of phospholipids and especially of phosphatidylcholine was found when alpha-glycerophosphate or lysolecithin served as the fatty acid acceptor. Glycerol and monoolein did not serve as fatty acid acceptors. More than 98% of the radioactivity was recovered as the rephosphatidylcholine fraction at the level of 0.64 micromoles/ml of lysolecithin in the incubation medium.

Animals↗

PubMed1982

Rat adipocyte utilization of different substrates: effects of cell size and the control of lipogenesis.

The metabolism of labeled glucose, pyruvate and acetate was compared in adipocytes isolated from old, obese rats (greater than 500 g) and young, lean rats (130-150 g). The larger cells from old, obese rats had markedly reduced rates of glucose, pyruvate and acetate conversion to glyceride-fatty acids, indicating that large cell fatty acid formation is reduced at some point beyond the entry of pyruvate and acetate into glucose metabolism. No evidence of a primary block in the pentose phosphate cycle of cells from old, obese rats was found. In spite of diminished glucose metabolism to several products in the large cells, both basal and insulin-stimulated rates of glyceride-glycerol synthesis from glucose and pyruvate were similar in each cell type. This indicates a relative diversion of carbon flow to alpha-glycerophosphate and reesterification in the large cells. Addition of low concentrations of glucose increase glyceride-fatty acid synthesis from acetate (both cell types) or pyruvate carbon (small cells), but decreased glyceride-glycerol synthesis from pyruvate carbon (both cell types). The acceleration of small cell fatty acid synthesis from pyruvate carbon by glucose and insulin was shown to be related to provision of NADPH from glucose metabolism in the pentose cycle. These studies indicate that, although the block in lipogenesis in adipocytes from old, obese rats appears to reside in the pathway of fatty acid synthesis itself, provision of additional alpha-glycerophosphate or NADPH from glucose metabolism may, under certain conditions, increase lipogenesis in cells from old, obese and young, lean rats.

6-Aminonicotinamide↗

PubMed1986

Mineralized bone nodules formed in vitro from enzymatically released rat calvaria cell populations.

Single-cell suspensions obtained from sequential enzymatic digestions of fetal rat calvaria were grown in long-term culture in the presence of ascorbic acid, Na beta-glycerophosphate, and dexamethasone to determine the capacity of these populations to form mineralized bone. In cultures of osteoblastlike cells grown in the presence of ascorbic acid and beta-glycerophosphate or ascorbic acid alone, three-dimensional nodules (approximately 75 micron thick) covered by polygonal cells resembling osteoblasts could be detected 3 days after confluency. The nodules became macroscopic (up to 3 mm in diameter) after a further 3-4 days. Only in the presence of organic phosphate did they mineralize. Nodules did not develop without ascorbic acid in the medium. Dexamethasone caused a significant increase in the number of nodules. Histologically, nodules resembled woven bone and the cells covering the nodules stained strongly for alkaline phosphatase. Immunolabeling with specific antibodies demonstrated intense staining for type I collagen that was mineral-associated, a weaker staining for type III collagen and osteonectin, and undetectable staining for type II collagen. Nodules did not develop from population I and the number of nodules formed by populations II-V bore a linear relationship to the number of cells plated (r = .99). The results indicate that enzymatically released calvaria cells can form mineralized bone nodules in vitro in the presence of ascorbic acid and organic phosphate.

Animals↗

PubMed1983

Characterization of the respiratory activity of mitochondria isolated from an insect cell line CP-1268 Laspeyresia pomonella.

Mitochondria have been isolated from the codling moth Laspeyresia pomonella, CP-1268 cell line. The mitochondrial fraction was isolated from pooled 4 d, exponential growth phase, cultures. The mitochondria were determined to be intact based on the demonstration of respiratory control, the effects of 2,4 dinitrophenol and oligomycin on respiration, the inability to oxidize NADH, and the inability of cytochrome c to enhance respiration. The isolated mitochondria were able to oxidize succinate, pyruvate, malate, alpha-ketoglutarate, and alpha-glycerophosphate efficiently. Of the substrates tested, the CP-1268 mitochondria oxidized succinate most efficiently. The respiratory control ratios ranged from a high of 4.6 for pyruvate to a low of 1.7 with alpha-glycerophosphate. These findings confirm that the mitochondria were tightly coupled. The data also confirm the presence of three sites of oxidative phosphorylation because NAD-linked substrates had ADP-to-O ratios approaching 3 and flavoprotein linked substrates had values approaching 2.

Animals↗

PubMed1976

Studies on the pathophysiology of acute renal failure. II. A histochemical study of the proximal tubule of the rat following administration of mercuric chloride.

Acute renal failure was induced in male rats by the subcutaneous injectioon of 4 mg HgC12 per kg body weight. Enzyme activities of the proximal tubule were studied histochemically at six time intervals from 15 min to 24 h. The enzyme studied were alkaline phosphatase, 5'-nucleotidase, acid phosphatase, alpha-glycerophosphate dehydrogenase (NAD-independent), malic dehydrogenase, succinic dehydrogenase, latic dehydrogenase, glucose-6-phosphate dehydrogenase and glucose-6-phosphatase. Decreases in activity were observed for alkaline phosphatase and 5'-nucleotidase after 15 min. Acid phosphatase was decreased after 30 min. These three enzymes returned to control levels after 3 h, but malic dehydrogenase and alpha-glycerophosphate dehydrogenase were decreased at this time interval. Succinic dehydrogenase was first decreased after 6 h. The earliest morphological changes detectable by light microscopy were observed in pars recta tubules in the medullary rays after 6 h, a time when all enzymes studied showed widespread decreased activity throughout the proximal tubule. After 24 h, the pars convoluta appeared morphologically normal but the pars recta was necrotic and exhibited calcification, whereas enzyme activity was decreased (absent in some cases) in both pars convoluta and pars recta. These results support the hypothesis that Hg++, when given in a sublethal dose, is associated with early histochemical changes in the brush border of the proximal tubule, which may be related to early changes in sodium reabsorption and to the subsequent development of acute renal failure. The observation that changes in plasma membrane-associated enzymes occur early and prior to alterations in enzymes of mitochondria and the endoplasmic reticulum suggests that Hg++ interacts initially with the plasma membrane.

Acute Kidney Injury↗

PubMed1994

Enzymatic, metabolic and secretory patterns in human islets of type 2 (non-insulin-dependent) diabetic patients.

Islets were isolated by automatic digestion from non-diabetic cadaveric organ donors and from Type 2 (non-insulin-dependent) diabetic subjects. The activity of FAD-glycerophosphate dehydrogenase, but not that of either glutamate dehydrogenase, glutamate-oxalacetate transaminase or glutamate-pyruvate transaminase, was lower in Type 2 diabetic patients than control subjects. Hexokinase, glucokinase and glutamate decarboxylase activities were also measured in islets from control subjects. The utilization of D-[5-3H]glucose, oxidation of D-[6-14C]glucose and release of insulin evoked by D-glucose were all lower in Type 2 diabetic patients than control subjects. The secretory response to the combination of L-leucine and L-glutamine appeared less severely affected. Islets from Type 2 diabetic patients may thus display enzymatic, metabolic and secretory anomalies similar to those often observed in animal models of Type 2 diabetes, including a deficiency of beta-cell FAD-linked glycerophosphate dehydrogenase, the key enzyme of the glycerol phosphate shuttle.

Adolescent↗

PubMed1998

Diabetes-induced changes in lens antioxidant status, glucose utilization and energy metabolism: effect of DL-alpha-lipoic acid.

The study was aimed at evaluating changes in lens antioxidant status, glucose utilization, redox state of free cytosolic NAD(P)-couples and adenine nucleotides in rats with 6-week streptozotocin-induced diabetes, and to assess a possibility of preventing them by DL-alpha-lipoic acid. Rats were divided into control and diabetic groups treated with and without DL-alpha-lipoic acid (100 mg x kg body weight(-1) x day(-1), i.p.). The concentrations of glucose, sorbitol, fructose, myo-inositol, oxidized glutathione, glycolytic intermediates, malate, alpha-glycerophosphate, and adenine nucleotides were assayed in individual lenses spectrofluorometrically by enzymatic methods, reduced glutathione and ascorbate--colorimetrically, and taurine by HPLC. Free cytosolic NAD+:NADH and NADP+:NADPH ratios were calculated from the lactate dehydrogenase and malic enzyme systems. Sorbitol pathway metabolites were found to increase, and antioxidant concentrations were reduced in diabetic rats compared with controls. The profile of glycolytic intermediates (increase in glucose 6-phosphate and fructose 6-phosphate, decrease in fructosel,6-diphosphate, increase in dihydroxyacetone phosphate, 3-phosphoglycerate, phosphoenolpyruvate, pyruvate, and no change in lactate), and 5.9-fold increase in alpha-glycerophosphate suggest diabetes-induced inhibition of glycolysis. Free cytosolic NAD+:NADH ratios, ATP levels, ATP/ADP x inorganic phosphate (Pi), and adenylate charge were reduced in diabetic rats while free cytosolic NADP+:NADPH ratios were elevated. Diabetes-induced changes in the concentrations of antioxidants, key glycolytic intermediates, free cytosolic NAD+:NADH ratios, and energy status were partially prevented by DL-alpha-lipoic acid, while sorbitol pathway metabolites and free cytosolic NADP+:NADPH ratios remained unaffected. In conclusion, diabetes-induced impairment of lens antioxidative defense, glucose intermediary metabolism via glycolysis, energy status and redox changes are partially prevented by DL-alpha-lipoic acid. The findings support the important role of oxidative stress in lens metabolic imbalances in diabetes.

Adenine Nucleotides↗

PubMed1992

Hydrophobic interaction chromatography fractionates lipoteichoic acid according to the size of the hydrophilic chain: a comparative study with anion-exchange and affinity chromatography for suitability in species analysis.

Hydrophobic interaction chromatography fractionated the lipoteichoic acid of Enterococcus faecalis into species of decreasing poly(glycerophosphate) chain length and decreasing extent of substitution with alpha-kojibiosyl residues (Glcp alpha 1----2Glcp alpha 1----). The chain length varied between 14 and 33 glycerophosphate residues per lipid anchor, the extent of glycosylation between 0.18 and 0.44 mol of alpha-kojibiosyl residues per mole of phosphorus, and, accordingly, the number of alpha-kojibiosyl substituents per chain between 3 and 15. Almost identical values were obtained when the same lipoteichoic acid was chromatographed on DEAE-Sephadex and concanavalin A, which separate molecular species according to increasing number of phosphate groups and alpha-kojibiosyl residues, respectively. Species from all three columns, which were identical in chain length and glycosylation, also had similar fatty acid patterns. These results prove the suitability of all three procedures for species analysis. One advantage of hydrophobic interaction chromatography over the other two procedures lies in its broader applicability since it is not dependent on negative charges or specifically binding oligosaccharide structures. Another advantage is the capacity of hydrophobic interaction chromatography to separate molecular species differing in the number of fatty acids [W. Fischer, H.U. Koch, and R. Haas (1983) Eur. J. Biochem. 133, 523-530] and render them accessible to molecular analyses.

Chromatography, Affinity↗

PubMed1987

Oxidation-reduction potentials and absorption spectra of two b-type cytochromes from the halophilic archaebacterium, Halobacterium halobium.

The oxidation-reduction midpoint potentials were determined for two b-type cytochromes, which had been solubilized from the membrane of Halobacterium halobium and partially purified. The two b-type cytochromes have oxidation-reduction midpoint potentials of 175 and 7 mV, respectively. These b-type cytochromes could also be resolved by difference absorption spectroscopy, which revealed one b-type cytochrome with absorption maximum (alpha-peak) at 558 nm, reducible by ascorbate-tetramethyl-p-phenylenediamine, and the other with absorption maximum (alpha-peak) at 560 nm, reducible by dithionite. Different substrates such as succinate, NADH, and alpha-glycerophosphate were used to study the b-type cytochromes in situ when bound to the membrane in a functional state. Reducing equivalents from succinate and alpha-glycerophosphate appear to enter the respiratory chain at the 175 mV b-type cytochrome. Cytochrome a3 is spectrophotometrically shown to be present in the membrane of H. halobium.

Cytochrome b Group↗

PubMed1990

Extramitochondrial release of hydrogen peroxide from insect and mouse liver mitochondria using the respiratory inhibitors phosphine, myxothiazol, and antimycin and spectral analysis of inhibited cytochromes.

The fumigant insecticide phosphine (PH3) is known to inhibit cytochrome c oxidase in vitro. Inhibition of the respiratory chain at this site has been shown to stimulate the generation of superoxide radicals (O2-), which dismutate to form hydrogen peroxide (H2O2). This study was performed in order to investigate the production of H2O2 by mitochondria isolated from granary weevil (Sitophilus granarius) and mouse liver on exposure to PH3. Other respiratory inhibitors, antimycin, myxothiazol, and rotenone were used with insect mitochondria. Hydrogen peroxide was measured spectrophotometrically using yeast cytochrome c peroxidase as an indicator. Insect and mouse liver mitochondria, utilizing endogenous substrate, both produced H2O2 after inhibition by PH3. Insect organelles released threefold more H2O2 than did mouse organelles, when exposed to PH3. Production of H2O2 by PH3-treated insect mitochondria was increased significantly on addition of the substrate alpha-glycerophosphate. Succinate did not enhance H2O2 production, however, indicating that the H2O2 did not result from the autoxidation of ubiquinone. NAD(+)-linked substrates, malate and pyruvate also had no effect on H2O2 production, suggesting that NADH-dehydrogenase was not the source of H2O2. Data obtained using antimycin and myxothiazol, both of which stimulated the release of H2O2 from insect mitochondria, lead to the conclusion that glycerophosphate dehydrogenase is a source of H2O2. The effect of combining PH3, antimycin, and myxothiazol on cytochrome spectra in insect mitochondria was also recorded. It was observed that PH3 reduces cytochrome c oxidase but none of the other cytochromes in the electron transport chain. There was no movement of electrons to cytochrome b when insect mitochondria are inhibited with PH3. The spectral data show that the inhibitors interact with the respiratory chain in a way that would allow the production of H2O2 from the sites proposed previously.

Animals↗

PubMed1975

Activation of bovine liver glycerol kinase by ethanol.

The crystallization of bovine glycerol kinase (ATP:glycerol 3-phosphotransferase EC 2.7.1.30) is reported along with a study on the unusual activation of this enzyme by ethanol. The enzyme was extracted from calf lever andusual activation of this enzyme by ethanol. The enzyme was extracted from calf liver and purified 5900-fold giving crystals with a 5% yield. The kinetics of the enzyme with regard to glycerol and ATP were studied by varying the concentration of one substrate while keeping the other at saturating levels, and the effect of ethanol was observed by adding it at levels of 5% (v/v). Ethanol increased the V in both cases almost 2-fold. The apparent Km of ATP was 3.5 - 10(-6) and was increased to 7.6 - 10(-6) in the presence of ethanol. The apparent Km for glycerol was 3 - 10(-5) and was increased to 12 - 10(-5) when ethanol was added. A number of other alcohols had a similar activating effect except for 1,2-diols which only inhibited the enzyme. These findings are consistent with the explanation that alcohols compete with glycerol (hence also with the glycerophosphate product) for a hydroxy binding site on the enzyme. This leads to more rapid dissociation of the glycerophosphate (i.e. an increase in the steady-state constant, "k+2" resulting in an increased V).

Adenosine Triphosphate↗

PubMed1977

Biochemical characterization of alkaline phosphatase in guinea pig thymus.

1. Alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) in guinea pig thymus was extracted optimally in 10 mM Tris - HCl buffer at pH 8.0 containing 5 g/l Triton X-100. 2. alpha-Glycerophosphate, beta-glycerophosphate and phenolphthalein monophosphate were hydrolyzed by thymus extract with a pH optimum at 9.8-10.0, whereas p-nitrophenylphosphate and alpha-naphthylphosphate were hydrolyzed with pH optima at 10.7-10.8 and beta-naphthylphosphate at pH 11.2. P-Nitrophenylphosphate and phenolphthalein monophosphate proved to be the most suitable substrates. 3. Alkaline phosphatase was effectively inhibited by EDTA, Zn2+, histidine and urea therefore resembling the inhibition characteristics of alkaline phosphatase in the placenta and kidney, but not that in the liver and intestine, which differed markedly. 4. DEAE-cellulose chromatography and polyacrylamide disc electrophoresis revealed three enzyme peaks which did not differ in their substrate specificities and modifier characteristics. 5. Polyacrylamide disc electrophoresis of thymus, serum, placenta, kidney, liver, bone and intestine revealed no alkaline phosphatase bands definitely unique to thymus.

Alkaline Phosphatase↗

PubMed1979

The stereoconfiguration of newly formed molecules of bis(monoacylglycero)phosphate in BHK cells.

Newly formed molecules of bis(monoacylglycero)phosphate (known also as lysobisphosphatidic acid), which were labeled with 32Pi in cultured BHK cells during relatively short pulses, were subjected to stereoanalysis. In contrast to the high proportion of sn-1-glycerophosphate residues in the bulk of the bis(monoacylglycero)phosphate molecules, the newly formed molecules were rich in sn-3-glycerophosphate residues.

Animals↗

PubMed1983

An enzymatic rationale for the randomization of the positional distribution of fatty acids in phospholipids of ascites hepatoma AH 130.

Fatty acids present in glycerophospholipids isolated from Yoshida ascites hepatoma AH 130 are more randomly distributed among the 1- and 2-positions than are fatty acids of normal liver phospholipids. The relative abundance of unsaturated fatty acids at the 1-position was ascribed to the lower palmitate-specific glycerophosphate acyltransferase activity in mitochondria of the hepatoma cells, an observation supporting the conclusion put forward for the similar randomization observed in Ehrlich ascites cells (Haldar, D., Tso, W.-W. and Pullman, M.E. (1979) J. Biol. Chem. 254, 4502-4509). The relative abundance of saturated fatty acids at the 2-position could be ascribed to the relatively lower acyl-CoA:1-acyl-glycerophosphocholine acyltransferase activity and to the change in the selectivity of the hepatoma acyl-CoA:1-acyl-glycerophosphate acyltransferase system into the lung type. The relatively lower selectivity for arachidonoyl-CoA as compared with oleoyl-CoA of the 1-acyl-glycerophosphocholine acyltransferase system is consistent with the decrease in polyenoic fatty acid content at the 2-position of the hepatoma phospholipids.

1-Acylglycerophosphocholine O-Acyltransferase↗