The cell differentiation system of Friend leukemia cells was applied to screening for new types of antitumor antibiotics. F5-5, Friend leukemia cells, were the most suitable for the assay system due to the stability of their response on repeated culture passages. Antibiotics like mitomycin C, adriamycin and actinomycin D, but not cycloheximide, did not induce detectable benzidine-positive cells among the F5-5 cells in the concentration ranges tested. Among the culture fluids of one thousand and fifty-one streptomycete strains subjected to the assay system, actinomycin V, FL-518 and FL-657 were found to be the most active as inducers. Actinomycin V possessing L-4-ketoproline as a substitute for L-proline of actinomycin D at a concentration of 1.0 ng/ml caused 39.7% of the F5-5 cells to become benzidine-positive. Furthermore, actinomycin V inhibited the colony formation of F5-5 cells in the soft agar medium at a concentration of 0.004ng/ml.

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The subsite structure of Thermoactinomyces vulgaris α-amylase was estimated from its action mode and rate parameters of hydrolysis on maltooligosaccharides. These results led to the conclusion that this α-amylase has six subsites with the catalytic site located between the third and fourth subsites from the non-reducing end side. Subsite affinities were calculated to be 0.38, 5.46, 2.72 and 0.23 kcal/mol for subsites 1, 2, 5 and 6, respectively, and the sum of the affinities of subsite 3 and 4 to be - 3.41 kcal/mol. The unique action mode of this α-amylase on various substrates was interpreted in terms of the subsite structure.

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Aminoacetonitrile (AAN), a specific inhibitor of glycine oxidation in the photorespiratory glycolate pathway, did not inhibit photosynthetic CO₂ fixation, but inhibited the apparent photosynthesis of rice leaves under high photosynthetic conditions. However, under such low photosynthetic conditions as low light intensity or senescent leaves, the apparent photosynthesis was not inhibited by AAN. The application of AAN to the leaves led to a greater accumulation of glycine under a high photosynthetic condition like strong light intensity.
From these results, it can be postulated that the inhibition of apparent photosynthesis by AAN was due to the accumulation of intermediate metabolites in the photorespiratory glycolate pathway which was induced by AAN treatment.

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A L-fucose-containing arabinogalactan-protein that strongly inhibited hemagglutination by eel anti-H agglutinin of human O erythrocytes was purified from hot phosphate-buffered saline extracts of mature leaves of rape, Brassica campestris. The purified glycoconjugate consisted of 90% of the polysaccharide moiety comprising L-fucose, L-arabinose, D-galactose, 4-O-methyl-D-glucuronic acid, and D-glucuronic acid, and 4% of the hydroxyproline-rich protein portion. Upon methylation, periodate oxidation, and enzymatic degradation, we found that consecutive β-(1→3)-linked D-galactopyranosyl residues constituted a backbone chain of the polysaccharide moiety, to which the side chains of β-(1→6)-linked D-galactopyranosyl residues were attached through O-6. Most of L-arabinofuranosyl residues were linked as single units through O-3 to the side chains while a small quantity of the sugar was present as (1→2)-, (1→3)-, or (1→5)-linked inter-chain residues. Single residues of α-L-fucopyranose, apparently attached to (1→2)-linked L-arabinofuranosyl residues, reacted with eel anti-H precipitin and Aleuria aurantia L-fucose-specific lectin, and were assumed to be crucial in the expression of the H-like activity. The uronosyl residues were also located at the non-reducing terminal ends. Reductive alkaline degradation of the arabinogalactanprotein provided indications that the polysaccharide chains were mainly conjugated through serine-O-glycosidic linkages to the polypeptide core. In an immunoprecipitation test, the rape leaf arabinogalactan-protein cross-reacted with antisera raised against radish leaf arabinogalactanprotein, indicating that these cruciferous arabinogalactan-proteins share common immunodeterminant(s) in their molecules.

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The possible regulation of dietary threonine intake and the effect of a palatable (sodium saccharin) or aversive (quinine sulfate) taste stimulus on the manner of threonine selection were investigated in rats using a self-selection feeding method. Weanling rats were offered the choice of two diets differing only in threonine content for 2 weeks. Both weight gain and food consumption in the rats offered the choice of diets were quite comparable to each other and were the same as those in rats fed one diet containing sufficient threonine. Threonine intake of the self-selecting rats ranged from 0.43 to 1.90% of the food consumed. The threonine concentrations in the plasma and brain of the self-selecting rats increased proportionally with the threonine intake. When rats were offered a choice of two diets containing various amounts of threonine with taste materials, i.e., sodium saccharin or quinine sulfate, neither the dietary threonine nor their growth were ever affected.
These results indicate clearly that rats have an ability to regulate threonine intake to meet their requirement for the L-amino acid, and the threonine selection is not influenced significantly by the dietary addition of palatable or aversive taste materials.

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The effect of the supplementation of sulfur amino acids to a low casein or soy protein isolate diet on tissue lipid metabolism was investigated. Supplementation of methionine to a 8% casein diet produced a fatty liver in rats, however, supplementation of methionine to a 8.8% soy protein diet (corresponding to a 8% casein diet as to sulfur amino acids content) did not produce a fatty liver. At the level of 8% or less of soy protein in the diet, the accumulation of liver lipids and serum triglyceride was observed. An amino acid mixture simulating the composition of soy protein isolate caused significant accumulation of liver lipids, but serum triglyceride was not changed. Serum cholesterol in rats fed the soy protein diet was lower than that in rats fed the casein diet, but on feeding the amino acid mixtures simulating these protein diets, there was no difference between the two groups. The small differences between soy protein isolate and casein as to lipid metabolism might be due to the small differences in the contents of sulfur amino acids or the specific nature of the soy protein or casein. The supplemental effect of methionine and cystine was also studied. About 60% of total sulfur amino acids could be substituted by cystine for maximum growth.

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The development of agar plate screening techniques has allowed the isolation of mutants of Trichoderma reesei capable of synthesizing cellulase under the conditions of a high concentration of glucose. Mutants resistant to catabolite repression by glycerol or glucose were isolated on Walseth's cellulose (WC) agar plates containing 5% glycerol or 5% glucose, respectively. Mutants resistant to catabolite repression by glycerol were not derepressed enough for the production of cellulase on WC agar plates containing 5% glucose or in flask cultures with a mixture of 1% Avicel and 3% glucose. On the contrary, two mutant strains resistant to catabolite repression by glucose (K.DD-10 and DGD-16) produced large clearing zones on WC agar plates containing 5% glucose. Both strains could begin to produce CMCase even in the presence of residual glucose and finally produced 1.5 times the CMCase activity, in flask cultures on 1% Avicel and 3% glucose, than that with 1% Avicel alone. These results suggest that KDD-10 and DGD-16 are comparatively derepressed by glucose for cellulase production.

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N-Benzoylglycine amidohydrolase (hippurate hydrolase EC 3.5.1.32), which catalyzes the hydrolysis of hippuric acid to benzoic acid and glycine, was found in a cell-free extract of Pseudomonas putida C692-3 grown on a medium containing hippuric acid. The enzyme was purified from the extract by ammonium sulfate fractionation and column chromatographies on DEAE-cellulose, DEAE-Sephadex A-50, hydroxyapatite, and Sepharose CL-6B. The enzyme was finally crystallized. The crystalline enzyme was almost homogeneous on electrophoresis. The enzyme had a molecular weight of about 170, 000 and consisted of four subunits identical in molecular weight (approximately 42, 000). The enzyme hydrolyzed N-benzoylglycine most rapidly, and _N-benzoyl-L-alanine and N-benzoyl-L-aminobutyric acid. The Km value for these substrates were 0.72mM, 0.87 mM, and 0.87mM, respectively. The optimum pH of the enzyme reaction was 7.0 to 8.0 and the enzyme was stable from pH 6.0 to 8.0.

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Several ionones and β-ionylideneacetic acids inhibited absicisic acid (ABA) biosynthesis in Cercospora rosicola at 100 μM. At lower concentrations, α-ionone, 1', 2'-dihydroxy-1', 2'-dihydro-β-ionone and 4'-keto-α-ionone enhanced ABA biosynthesis. Conversions of ionones by C. rosicola were identified by GC-MS as: α-ionone to 4'-keto-α-ionone, 4'-keto-α-ionol and dehydrovomifoliol; and 1'-hydroxy-α-ionone to dehydrovomifoliol. The oxidations of α-ionone and its analogs parallel those of the α-ionylideneacetic acids. The β-ionylideneacetic acids were generally oxidized to more polar forms. Metabolites identified by GC-MS were 3'-hydroxy-, 3'-keto- and 1', 2'-epoxy-1', 2'-dihydro-β-ionylideneacetic acids. The fungus rapidly metabolized most exogenous materials to more polar forms.

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Farnesyl and α-ionylideneethyl compounds with tertiary and quaternary amine functional groups were synthesized and their effects on abscisic acid (ABA) biosynthesis of Cercospora rosicola observed. The trimethylammonium compounds were lethal at 100μM and inhibitory at 10 μM, but lesser amounts of α-ionylideneethyltrimethylammonium iodide enhanced ABA biosynthesis. N, N-Dimethylfarnesylamine had little effect on ABA biosynthesis. N, N-Dimethyl (2Z, 4E)- and (2E, 4E)-α-ionylideneethylamines inhibited ABA biosynthesis at 100μM but had no or little effect at lower concentrations. Farnesol and farnesylpyrophosphate (FPP) enhanced ABA biosynthesis. FPP appears to be both a precursor and an inducer and farnesol is an inducer of ABA biosynthesis. N, N-Dimethyl (2Z, 4E)- and (2E, 4E)-α-ionylideneethylamines were converted to N, N-dimethyl (2Z, 4E))- and (2E, 4E)-4'-keto-α-ionylideneethylamines, respectively. These conversions are analogous to those reported for α-ionone and α-ionylideneacetic acids and show that basic as well as acidic and neutral compounds with α-ionone type rings can undergo oxidation at the 4'-position. α-Ionylideneacetic acids inhibited growth of C. rosicola and the dimethylamines enhanced growth. Complete feedback inhibition was obtained with 400 μM of ABA.

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The effect of dietary fat on tryptophan-NAD metabolism was investigated. Weanling male rats of the Sprague Dawley strain were fed a 40% casein diet (nicotinic acid-free) with or without 20% fat for 13 days. Although the food intake in 13 days was significantly higher in the fat-free group than in the fat group, the gains in body weight in the two groups were almost the same, because of the same energy intakes. The urinary excretion of tryptophan metabolites such as quinolinic acid, niacin and N¹-methylnicotinamide was greatly increased in the fat group in comparison with that in the fat-free group. The urinary excretion of xanthurenic acid was almost the same in the two groups. The blood NAD level of the fat group was significantly increased. The activities of liver amino-carboxymuconate-semialdehyde decarboxylase and liver nicotinamide methyltransferase in the fat group were significantly reduced, and that of liver NMN adenylyltransferase was significantly increased. The changes of these three enzymes could be advantageous for the increased formation of NAD from tryptophan. As a result, the feeding of a high fat diet to rats increased the formation of niacin and niacin-related compounds.

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For the purpose of enzymatic preparation of ADP-glucose (ADPG), bacterial screening was performed to find a strain having a high activity of ADPG pyrophosphorylase which catalyzes the synthesis of ADPG from ATP and glucose-1-phosphate. A cell-free extract of Arthrobacter simplex IFO 12069 showed a strong enzyme activity for the synthesis of ADPG, which was isolated from the reaction solution by ion-exchange column chromatography and identified by paper and thin-layer chromatography. The enzyme activity of the bacterium reached a maximum in the late logarithmic phase under aerobic growth conditions. Some factors affecting the ADPG synthesis, e.g. reaction pH, substrate concentrations, divalent cations, inhibitors and activators, were studied with an ammonium sulfate fraction, 30-50% saturation as the enzyme preparation.

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Theanine hydrolase activity in tea leaves was assayed by measuring enzymatically released ethylamine from L-theanine. The o-phthalaldehyde derivative of ethylamine was measured by reverse phase HPLC recorded with a spectrofluorometric detector.
Theanine hydrolase activity was purified about 4.6-fold by DEAE-cellulose column chromatography. Although this active fraction also had glutaminase activity, the yield of the glutaminase activity was about 50% of that of theanine hydrolytic activity. The theanine hydrolytic activity was inhibited by acidic amino acid and L-alanine, and stimulated by L-malic acid. The purified enzyme solution hydrolyzed not only theanine but also γ-glutamylmethylamide, γ-glutamyl-n-propylamide, γ-glutamyl-n-butylamide, γ-glutamy-iso-butylamide, and γ-glutamyl-n-amylamide, which were synthesized from L-pyroglutamic acid and corresponding alkylamines. However, N-methylpropionamide and N-ethylpropionamide were not hydrolyzed. The theanine hydrolase activity and glutaminase in tea leaves showed the same pH optimum (8.5).
The activity of theanine hydrolase in tea leaves increased during the first 10hr after plucking but then decreased gradually, while that of glutaminase decreased constantly and was almost lost 48 hr after plucking.

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(2R^*, 4S^*, 6S^*, αS^*)- and (2R, 4R, 6R, αS)-Streptovitacin-C₂ (STV-C₂) (1a and 1b) were synthesized by an aldol condensation of (2R^*, 4S^*)- or (2R, 4R)-2, 4-dimethyl-2-trimethylsiloxy-1-cyclohexanone (15a or 15b) with 4-(2-oxoethyi)-2, 6-piperidinedione (16), which was followed by desilylation of the products. The stereochemistry of the synthesized STV-C₂ isomers (1a and 1b) was elucidated by NMR. STV-C₂ isomers (1a and 1b) did not show strong antimicrobial activity against Saccharomyces cerevisiae and Pyricularia oryzae.

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The chorismate mutase and prephenate dehydratase genes of phenylalanine producing Corynebacterium glutamicum K38, which is resistant to p-fiuorophenylalanine and m-fluorophenylalanine, were cloned into plasmid pCE53 in C. glutamicum KY9456, which lacks chorismate mutase and prephenate dehydratase. One of the resultant plasmids, pCmB4, contained a 9.4kb Bam HI DNA fragment inserted into the unique BamHI site of pCE53. Plasmid pCmB4 complemented a phenylalanine and tyrosine double auxotroph of C. glutamicum KY9456. Introduction of pCmB4 into C. glutamicum RRL5 resulted in an about ten times increase in chorismate mutase activity. C. glutamicum K38 carrying the plasmid accumulated 19.0mg/ml of phenylalanine (50% increase over the yield of K38).

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The behavior toward oxygen of several strains of Pediococcus halophilus was studied. Although these organisms are generally regarded as facultative anaerobes, this investigation showed that resting cells of P. halophilus consumed oxygen at the expense of p-glucose or L-lactate as substrate.
The oxygen consuming activities among strains of soy pediococci varied from 7.06 to 11.63 (nmol/min/mg dry cells) with glucose and 5.52 to 6.59 with L-lactate, respectively. Oxidative metabolism of glucose increased acetate production with a corresponding decrease in lactate formation. Lactate oxidation with O₂ led to the formation of acetate. The oxygen consuming activity was not inhibited by any of the respiratory inhibitors tested such as KCN or NaN₃.
NADH oxidase activity was found in cell-free extracts of P. halophilus No. 51, which is capable of lowering the redox potential of the growth medium. A direct correlation between the abilities to consume oxygen and to reduce the redox potential has not been found so far, but this enzyme is considered to be involved in the aerobic metabolism.

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NADH-dependent soluble L-α-hydroxyglutarate dehydrogenase (L-2-hydroxyglutarate: NAD⁺ 2-oxidoreductase) was found in a bacterium belonging to the genus Alcaligenes obtained from soil by citrate enrichment culture. A mutant with about 2.5-fold higher activity of the enzyme was derived from the bacterium and used as the enzyme source. High level of the enzyme was produced at the late stage of cultivation in the presence of citrate and with limited aeration. The enzyme was purified from the cells to homogeneity to give crystals, and its enzymatic properties were studied. The enzyme strongly reduced α-ketoglutarate to stereochemically pure L-α-hydroxyglutarate with NADH as a coenzyme, but it oxidized D-α-hydroxyglutarate with about 1/10 of the rate for L-form oxidation.

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To examine the origin of urinary hydroxyproline peptides, the metabolism of the radioactive tripeptide, glycyl-¹⁴C-prolylhydroxyproline, was investigated in normal young rats in vivo. The radioactive tripeptide was synthesized from glycine, L-(U-¹⁴C)proline and hydroxy-L-proline in our laboratory. The distributions of the radioactivity in body protein, lipid and soluble fractions were 23.7, 1.8 and 0.12% of the injected dose, respectively, 56 hr after the intraperitoneal injection of the ¹⁴C-tripeptide. The excretions of the radioactivity into expired carbon dioxide and urine were 29.6 and 34.2% of the injected dose, respectively, and large proportions of both the ¹⁴C excretions occurred during the first 12hr.
The results suggest that not a small amount of the glycylprolylhydroxyproline peptide injected is hydrolyzed in tissues of animals and the free proline derived is used for protein synthesis and/or further degraded to expired carbon dioxide.

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Pumpkin (Cucurbita moschata) ascorbate oxidase was entrapped within 6% (w/v) Ca-alginate gel beads, and then the beads were treated with 1% (w/v) glutaraldehyde for 20 hr at 4°. The immobilized ascorbate oxidase was much more stable than the free form. Under the optimum conditions, the immobilized enzyme remained fully active for 3 months and after 50 assays. A linear relationship was found between immobilized ascorbate oxidase activity and L-ascorbic acid concentration in the range of 2-20 μg/ml. The immobilized preparation could be employed for the simple and rapid determination of L-ascorbic acid in foods.

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Bromoperoxidases were found in coralline algae (Corallinaceae, Rhodophyta) collected from seasides in Japan, and high enzyme activities were observed in Corallina officinalis, Corallina pilulifera and Amphiroa zonata. The optimum pHs of the enzymes from coralline algae were around 6.0. The enzymes were specific for I^- and Br^-, and did not act on Cl^- and F^-. The enzymes purified from Corallina pilulifera and Amphiroa ephedraea catalyzed the brominations of phenol and o-hydroxybenzyl alcohol in the presence of Br^- and H₂O₂ to form the same product, 2, 4, 6-tribromophenol.

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The structure of a new indole derivative, serotobenine (1), from safflower meal (Carthamus tinctorius L.) is proposed based on ¹H- and ¹³C-NMR spectral data and X-ray crystallography. The known compounds N-feruloyltryptamine (2) and N-(p-coumaroyl)tryptamine (3) were also isolated and identified.

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Some physicochemical and functional properties of cardiac myosin were studied in a model system, with particular reference to its binding ability in re-structured meat. We found that myosin solubility was strongly influenced by the pH, ionic strength, and temperature of the system and by the interaction of pH and ionic strength. For instance, myosin remained completely in solution in monomeric form at ionic strengths ?? 0.2M KCl, if the pH of system was maintained at 7.0. High ionic strength was required to keep myosin in monomeric form at low pH. With low ionic strength and pH, myosin molecules tend to form aggregated filaments.
Like skeletal muscle myosin, the heat-induced gel strength of cardiac myosin was also influenced by the pH, ionic strength, and temperature of the system, and it produced a gel with maximum strength (21 × 10³dyn/cm²) at pH 5.5 and 0.1 M KCl concentration on heating to 60°C. Cardiac myosin seems to form much stronger gels than skeletal muscle myosin.

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Three new trisaccharide-azoxyglycosides were formed from some azoxyglycosides by transglucosylation by a β-D-glucosidase from cycad seeds. These azoxyglycosides, named neocycasin H, I, and J, were identified as O-β-D-glucopyranosyl-(1→4)-O-β-D-glucopyranosyl-(1→3)-O-β-D-glucopyranoside of methylazoxymethanol (MAM), O-β-D-glucopyranosyl-(1→3)-[O-β-D-glucopyranosyl-(1→6)]-O-β-D-glucopyranoside of MAM, and O-β-D-glucopyranosyl-(1→3)-[O-β-D-xylopyranosyl-(1→6)]-O-β-D-glucopyranoside of MAM, respectively. On the basis of their structures, the mechanism of the formation of these neocycasins is also discussed.

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Both D- and L-α-amino-δ-valerolactam inactivated α-amino-ε-caprolactam racemase during incubation with the enzyme. The degree of inactivation increased with increases in pH and the concentration of L-α-amino-δ-valerolactam in the incubation mixture. Pyridoxal 5'-phosphate reactivated the inactivated enzyme, and glyoxylate and other α-keto acids such as pyruvate, phenylpyruvate, and α-ketobutyrate protected the enzyme from inactivation by L-α-amino-δ-valerolactam. Both the enantiomers of methionine were produced when α-keto-γ-methylthiobutyrate was incubated with the enzyme in the presence of L-α-amino-δ-valerolactam. Thus, the inactivation of the enzyme in terms of a-amino-ocaprolactam racemization activity is due to conversion of the enzyme-bound pyridoxal 5'-phosphate into pyridoxamine 5'-phosphate by a transamination with L-α-amino-δ-valerolactam. Formation of pyridoxamine 5'-phosphate from the enzyme-bound pyridoxal 5'-phosphate was proved by spectrophotometry and thin layer chromatography. The rate of racemization of L-α-amino-δ-valerolactam was calculated to be 48 times faster than that of the transamination with glyoxylate.

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Chemical synthesis of long-chain oligodeoxyribonucleotides was studied by the method of block condensation in a liquid phase. A method for elongating the chain and the synthesis of oligothymidylic acids up to 80-mer are described.

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Most of the glycoproteins were extracted selectively from bovine milk fat globule membrane (MFGM) and MFGM-apoprotein with lithium diiodosalicylate (LDS). By partitioning the LDSextracts with phenol, the glycoproteins were separated into two phases: the upper LDS-aqueous phase and the lower phenol phase. Special attention was paid to the glycoproteins partitioned in the latter and the characteristics of the fractions were compared. Of the major glycoproteins stained with periodic acid-Schiff reagent (PAS), PAS-1, 2, and 3 bands were extracted in the LDS-aqueous phase and PAS-4, 6 and 7 bands into the phenol phase. PAS-5 was not extracted with LDS. Of glycopeptides constituting the soluble glycoprotein, PAS-8 and 9 bands were partitioned into the aqueous phase, but PAS-10 and 11 into the phenol phase. The glycoprotein partitioned in the phenol fraction was relatively rich in hexoses and had fewer hydrophilic amino acid residues, and a high absorption coefficient (13.6), while that of the LDS-aqueous phase was rich in sialic acid and hydrophilic amino acid residues and had a lower absorption coefficient (4.1).

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Plasmid pCX311, which we constructed, has two HindIII DNA fragments (2.6kbp and 2.Qkbp) of alkalophilic Bacillus sp. strain C-125 in the HindIII site of pBR322.
These two fragments were essential not only for the xylanase production but also for the excretion of periplasmic proteins. The cloned 4.6 kbp fragment encodes some components that made the outer membrane of E. coli permeable. Some proteins such as xylanase and β-lactamase were excreted, but alkaline phosphatase was not excreted into the culture broth.

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A type II restriction endonuclease, designated as GceGLl, was purified from cells of Gluconobacter cerinus IFO 3285. The purified enzyme was found to be homogeneous on polyacrylamide gel disc electrophoresis. The enzyme worked best at 37°C and pH 7.5 and required 7 mM MgCl₂ and 100 mM NaCl. The purified enzyme was stable when preincubated over a pH range of 7.5 to 9.5 for 12hrat 4°C and a temperature range of 37 to 40°C for 5min at pH 7.5. The enzyme was shown to cleave λ, φX174 RF, SV40, pBR322, M13 mp7 RF and Ad2 DNAs at 4, 1, 0, 0, 0 and 25 or more sites, respectively, and to recognize the DNA sequence of 5'-C-C-G-C-G-G-3' and to cut between C and G on the right side of the sequence, being an isoschizomer of SacII of Streptomyces achromogenes ATCC 12767.

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Various α-isocyanocycloalkylideneacetamides were synthesized by the reaction of isocyanoacetamides with ketones and following by dehydration. These compounds were examined for their inhibitory activity against the germination of rice, cucumber and radish seeds, and for their herbicidal effects on rice, tomato and weed seedlings. Among them, α-isocyanocyclohexylideneacetylpiperidine showed selective herbicidal activity against the broad-leaf plants.

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Syntheses of three optically active pyrethroids containing cinnamyl-type alcohol moieties, and their insecticidal activity are reported. The presence of a m-phenoxy group at a benzene ring inverted the structure-activity relationships dramatically with respect to the absolute configuration of alcohol moieties.

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