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Modification with acetic anhydride of nucleosomes from chicken erythrocytes at low ionic strength (less than 0.1 M NaCl) is accompanied by the formation of residual particles and the release of free DNA. This DNA has been identified as single-stranded by thermal denaturation, digestion with nuclease S1, and elution from hydroxyapatite. In contrast, if modification takes place at 0.6 M NaCl, the liberated DNA is mainly double-stranded. The release of the free energy stored in folded nucleosomal DNA, triggered by the weakening of lysine-DNA interactions which takes place upon modification, might be responsible for the observed denaturation of DNA at low ionic strength.
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Etherification of butanol by acetic anhydride in butanol-butyl acetate mixtures containing 0.09 to 3 per cent water was investigated. A method for processing the butanol-butyl acetate mixtures with the weight part of butanol up to 16 per cent by etherification of the latter with acetic anhydride was developed, the yield being 96 to 97 per cent and the weight part being at least 97.5 per cent. On the basis of the estimate of the raw material use for regeneration of butyl acetate from the butanol-butyl acetate solutions by etherification of butanol with acetic anhydride, the technical and economic advantages of the processing of such solutions by the described method were shown.
Treatment of 9,2'-diacetylmidecamycin (2) with DMSO and acetic anhydride afforded 3''-methylthiomethyl derivative (3) preferably in the presence of pyridine. Reaction of midecamycin (1) with DMSO and acetic anhydride gave 2'-acetyl-9-dehydro-3''-methylthiomethyl derivative (9) indicating that the three hydroxyl groups reacted in a different way to the reagent. When compound 2 was reacted with DMSO and acetic anhydride in the presence of CCl4, 3''-acetoxymethyl derivative (13) was a major product, which was formed via 3 through the Pummerer rearrangement. The structures of 3, 9 and 13 were confirmed by examining NMR and mass spectra of these compounds and their deuterio analogue. They showed antimicrobial spectra similar to 1 but superior in vivo activity.
This paper describes the development of a new method for monitoring acetic anhydride in the presence of acetic acid in the occupational environment. The method consisted of collecting airborne acetic anhydride on a solid sorbent, desorbing it with acetone and analyzing it by gas chromatography. During the development of this method various parameters such as selection of column, selection of solid sorbent, selection of desorber solvent, effects of humidity, flow rate, total sample volume, desorption efficiency, and shelf-life of samples were studied. Interference from methyl acetate, water, formic acid, and acetic acid was also tested with the determination of acetic anhydride.
Analytical methods based on the title reactions are reviewed, and the malonic acid-acetic anhydride system was selected for detailed study. It is postulated that carbon suboxide, O = C = C = C = O, formed by the action of acetic anhydride on malonic acid, is the effective reactive species in this system. Carbon suboxide was prepared and identified, and spectrophotometric observations of its reactions with tertiary amines are described. Aliphatic and aromatic tertiary amines generate colored products upon reaction with carbon suboxide in the presence of acetic anhydride. It was found that aliphatic tertiary amines form colors upon reaction with carbon suboxide in the absence of acetic anhydride, whereas aromatic tertiary amines require the presence of acetic anhydride.
We describe a convenient, rapid, and reproducible method for labeling proteins in vitro by acetylation with [3H] or [14-C]acetic anhydride dissolved in small amounts of anhydrous dioxane. The reaction is carried out at neutral pH and does not require the use of detergents, water-immiscible organic solvents, oxidizing, or reducing agents. Thus undesirable solvent-induced alterations in protein structure and biological activity are minimized. A method for calculating the specific activity of the protein and the efficiency of acetylation at known concentrations of protein and acetic anhydride is presented. Radioacetylated proteins were shown to be suitable for use as molecular weight calibration standards and as protein markers in polyacrylamide gel electrophoresis, gel filtration, and enzyme studies. Acetic anhydride was used to label intact oncornaviruses, which consist of a complex ribonucleo-protein core within a lipid envelope. Some of the viral lipid and all of the viral proteins, including the internal ones, were labeled without detectable alterations in viral morphology or buoyant density. This result suggests that acetic anhydride, evidently by virtue of its small size and neutral charge, penetrates freely throughout the viral membrane and core structures. The reactivity of RNA with acetic anhydride was less than 1% that of protein under similar reaction conditions.
1. Reactivation of deacetyl citramalate lyase by acetic anhydride proceeds through an enzyme-anhydride complex prior to actual acetylation. The reaction is inhibited by citramalate which is competitive with acetic anhydride. 2. A corresponding complex is an intermediate in the carboxymethylation of deacetyl enzyme by iodoacetate. However, the inhibition of this reaction by S-citramalate appears to be non-competitive with iodoacetate. 3. The results lead to the conclusion that acetic anhydride can be regarded as a structural analogue of citramalic acetic anhydride, the proposed intermediate in the acyl exchange reaction on citramalate lyase. 4. The formation of 6-citryl thiolester from the 1-thiolester via the cyclic citric anhydride provides a chemicla model for enzymic acyl exchange. 5. The data suggest that anhydrides are of general importance in acyl exchange reactions of thiolesters.
Acetylation with acetic anhydride, under both aqueous and anhydrous conditions, has been utilized to derivatize various biogenic amines and psychotropic drugs for subsequent analysis by gas chromatography (GC) or gas chromatography-mass spectrometry (GC-MS). Under basic aqueous conditions, acetic anhydride derivatizes phenols and amines but not alcohols; under anhydrous conditions, all three functions are acetylated. Primary amines, once derivatized with acetic anhydride, can be further derivatized with other reagents; these diderivatives have proven useful for subsequent analysis by GC or GC-MS. Examples of applications of derivatization with acetic anhydride to analysis of biogenic amines, antidepressants, antipsychotics, and some of their metabolites are presented.
The sensitivity of radioimmunoassays for cyclic AMP and cyclic GMP has been markedly improved to readily detect femtomole (10-15) amounts in tissue extracts by acetylating the cyclic nucleotides at the 2'0 position with acetic anhydride. Acetylation of cyclic nucleotides by acetic anhydride in aqueous solution proceeds more rapidly than the hydrolysis of acetic anhydride to acetic acid thus yielding 100% acetylated cyclic nucleotide. 2'0 substituted cyclic nucleotides have greater affinity for the antibody than the parent cyclic nucleotides because the antibody has been made to a protein conjugate coupled at the 2'0 position. This simple acetylation technique makes it possible to measure cyclic AMP and cyclic GMP in minute quantities of tissue without purification or concentration of the sample.
A successive C-terminal amino acid truncation reaction with acetic anhydride was applied on proteins in polyacrylamide gel. Protein bands separated by conventional SDS-PAGE were excised, partially fixed in the gel with glutaraldehyde ethanol solution, dehydrated with ACN and subjected to the truncation reaction with acetic anhydride formamide solution. Pre-treatment of the gel with pyridine aqueous solution was found to enhance the truncation reaction yields. After the truncation reaction, the products were treated with an aqueous solution of dimethylaminoethanol to hydrolyze oxazolone rings at the C termini of the truncated products and O-acetylated products of serine, threonine and/or tyrosine. Several commercially available proteins of 10-40 kDa, as determined by SDS-PAGE, such as myoglobin, trypsin inhibitor, alpha-hemolysin, cytochrome c, chymotrypsin C chain, elastase, acylase and histone H4, were subjected to the C-terminal analysis. The truncated proteins were in-gel digested with trypsin and the extracted peptides were analyzed by MALDI-TOF MS, giving rise to a series of molecular mass ions of the C-terminal truncated fragments corresponding to the C-terminal amino acid sequence of the relevant protein.
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The applicability of acetic anhydride (AA) in dimethyl sulfoxide (DMSO) for the oxidation of polysaccharide and their subsequent visualization with thiocarbohydrazide (TCH) and silver proteinate (SP) was evaluated on LR White-embedded thick and ultrathin liver sections. The results of these studies indicated that AA-DMSO-TCH-SP reaction is chemically specific on LR White-embedded tissues and that it offers distinct advantages for the localization of minute glycogen aggregates.