Dimethylmaleic Anhydride Research Articles

Purification and reconstitution of the adipocyte plasma membrane D-glucose transport system

Rat adipocyte plasma membranes have previously been shown to retain stereospecific transport activity for D-glucose following extraction of extrinsic proteins with dimethylmaleic anhydride (Shanahan, M. F., and Czech, M. P. (1977) J. Biol. Chem. 252, 6554-6561). When these extracted plasma membranes were incubated in 2% sodium cholate and centrifuged, the resultant supernatant contained only one major glycoprotein fraction of 94,000 daltons, as determined by dodecyl sulfate-polyacrylamide gel electrophoresis. This protein fraction was combined with cholate-dispersed, exogenous phospholipids. The detergent was removed by gel filtration and vesicles composed of phospholipid and membrane protein were formed which exhibited preferential, time-dependent uptake of D- versus L-glucose when measured by a rapid filtration method. In addition, D-glucose uptake was inhibited by cytochalasin B, phlorizin, phloretin, and dipyridamole. These results suggest the direct involvement of the 94,000-dalton glycoprotein fraction in fat cell hexose transport.

Rate constants of the permanganate oxidation of dimethylmaleic acid and dimethylmaleic anhydride

Rate constants of the permanganate oxidation of dimethylmaleic acid and dimethylmaleic anhydride

Differential phosphorylation of band 3 and glycophorin in intact and extracted erythrocyte membranes

AbstractThis report presents an analysis of the phosphorylation of human and rabbit erythrocyte membrane proteins which migrate in NaDodSO4‐polyacrylamide gels in the area of the Coomassie Blue‐stained proteins generally known as band 3. The phosphorylation of these proteins is of interest as band 3 has been implicated in transport processes. This study shows that there are at least three distinct phosphoproteins associated with the band 3 region of human erythrocyte membranes. These are band 2.9, the major band 3, and PAS‐1. The phosphorylation of these proteins is differentially catalyzed by solubilized membrane and cytoplasmic cyclic AMP‐dependent and ‐independent erythrocyte protein kinases. Band 2.9 is present and phosphorylated in unfractionated human and rabbit erythrocyte ghosts but not in NaI‐ or dimethylmaleic anhydride (DMMA)‐extracted membranes. These latter membrane preparations are enriched in band 3 and in sialoglycoproteins. The NaI‐extracted ghosts contain residual protein kinase activity which can catalyze the autophosphorylation of band 3 whereas the DMMA‐extracted ghosts are usually devoid of any kinase activity. However, both NaI‐ and DMMA‐extracted ghosts, as well as Triton X‐100 extracts of the DMMA‐extracted ghosts, can be phosphorylated by various erythrocyte protein kinases. The kinases which preferentially phosphorylate the major band 3 protein are inactive towards PAS‐1 while the kinases active towards PAS‐1 are less active towards band 3. The band 3 protein in the DMMA‐extracted ghosts can be cross‐linked with the Cu2+ ‐σ‐phenanthroline complex. The cross‐linking of band 3 does not affect its capacity to serve as a phosphoryl acceptor nor does phosphorylation affect the capacity of band 3 to form cross‐links. In addition to band 2.9, the major band 3 and PAS‐1, another minor protein component appears to be present in the band 3 region in human erythrocyte membranes. This protein is specifically phosphorylated by the cyclic AMP‐dependent protein kinases isolated from the cytoplasm of rabbit erythrocytes. The rabbit erythrocyte membranes lack PAS‐1 and the cyclic AMP‐dependent protein kinase substrate.

Pyrogenesis of succinic acid and dimethylmaleic anhydride from aspartic acid

Pyrogenesis of succinic acid and dimethylmaleic anhydride from aspartic acid

Preparative isolation of Band 3, the predominant polypeptides of the human erythrocyte membrane

Band 3 proteins are the predominant polypeptide components of the human erythrocyte membrane and have been implicated in various transport activities. Following extraction of membrane ghosts with dimethylmaleic anhydride to remove two polypeptides (Bands 4.2 and 6) associated with Band 3, Band 3 proteins were solubilized along with the other major membrane glycoproteins (PAS 1–3) with Triton X-100 under nondenaturing conditions. Band 3 proteins were then purified (>95%) on a large scale by chromatography via thioldisulfide interchange on activated thiol-Sepharose 4B [agarose-(glutathione-2-pyridyl disulfide) conjugate]. This procedure allows the preparation of 20 to 25 mg of purified Band 3 proteins in high yield (>80%) from ghosts in a soluble form suitable for physical, chemical, and functional characterization.

The vibrational spectra of monomethyl and dimethyl maleic anhydride

The i.r. spectra of monomethyl and dimethyl maleic anhydride were studied in all three physical states in the region 5000-50 cm −1. Raman spectra of monomethyl maleic anhydride as a liquid and dimethyl maleic anhydride in solution and as a solid were also investigated. The fundamental frequencies have been assigned and force constant calculations have been performed.

Dissociation of bovine 6S procarboxypeptidase A by reversible condensation with 2,3-dimethyl maleic anhydride: application to the partial characterization of subunit III.

Bovine 6S procarboxypeptidase A can be dissociated into its three subunits by acylation with dimethyl maleic anhydride. The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same residues in bovine chymotrypsinogen A and C (subunit II) and also in proelastase A of the African lungfish. Therefore, this subunit is likely to be a chymotrypsinogen or proelastase-A-like zymogen which has lost the ability to be activated on account of a deletion of the N-terminal residues from half-cystine 1 to valine 17. Like other pancreatic zymogens, subunit III appears to possess a weakly functional active site.

Binding of cytochalasin B to a red cell membrane protein

Dimethyl maleic anhydride was used to solubilize all of the major membrane proteins of the human red blood cell except band 3, band 7, and glycophorin. The extracted membrane contains all of the sugar transport-related cytochalasin B binding sites of the cell. Binding of cytochalasin B is inhibited by p-chloromercuribenzoate or by p-chloromercuribenzene sulfonate and this inhibition is reversed by 2-mercaptoethanol, showing that sulfhydryl groups are involved in the cytochalasin B binding reaction. This result and other observations suggest that the sugar transport-related cytochalasin B binding sites are most likely associated with the band 3 protein.

Structural effects on the rates of formation of amic acids and imides

The reaction of amines with maleic anhydride (MA), pyromellitic anhydride (PMDA), dimethylmaleic anhydride (DMMA), and cyclo-octa-1,5-diene- 1,2,5,6-tetracarboxylic dianhydride (CODA) was followed by titration. MA and PMDA give the amic acids very readily and cyclize to the imides only at high temperatures, while DMMA and CODA react slowly to yield a mixture of the amic acids and imides even at ambient temperatures. The structural factors affecting the reaction are discussed.

Ring expansion of 3-acetylcoumarin by diazoethane: lactones derived from oxepin, oxocin, and oxonin

Diazoethane partly alkylates 3-acetylcoumarin giving 3-acetyl-4-ethylcoumarin, and partly expands the lactone ring giving, after addition of a second molecule of diazoethane, the benzoxepinopyrazoline (IX) as a racemate of assigned stereochemistry. This compound readily loses nitrogen and undergoes a second ring expansion to form the benzoxocin derivative (XII) as a single (racemic) stereoisomer. Treatment of (XII) with diazoethane induces immediate ring expansion giving the benzoxonin derivative (XIII), again as a single (racemic) stereoisomer. There is no further reaction with diazoalkanes, notwithstanding the presence of a highly activated double bond; the resistance is attributed to the internal compression that would result within a highly convoluted molecule if addition occurred.The structures and conformations of the foregoing products and of some by-products have been established by spectroscopic methods. Additionally, the benzoxocin derivative (XII) has been shown to yield meso-dimethyl-succinic acid upon exhaustive ozonolysis, and a convenient method is described for the preparation of small amounts of dimethylmaleic anhydride by the reaction of diazomethane with methylmaleic anhydride.A parallel is drawn between these reactions and certain of those found with quinone–diazoalkane adducts, and it is suggested that ring expansions are observed because the methyl group introduced with the diazoethane molecule forces the pyrazoline into the necessary conformation.

Structure and efficiency in intramolecular and enzymic catalysis. Catalysis of amide hydrolysis by the carboxy-group of substituted maleamic acids

The efficiency of intramolecular catalysis of amide hydrolysis by the carboxy-group of a series of substituted N-methylmaleamic acids is remarkably sensitive to the pattern of substitution on the carbon–carbon double bond. A single alkyl group increases the rate of hydrolysis by a factor which increases with its size. A second alkyl substituent has a disproportionately larger effect, which is sharply reduced when the two groups are joined together in a ring. The rates of hydrolysis of a series of dialkyl-N-methylmaleamic acids range over more than ten powers of ten, and the ‘effective concentration’ of the carboxy-group of the most reactive compound studied is greater than 1010M. This amide, dimethyl-N-n-propylmaleamic acid, is converted into the more stable dimethylmaleic anhydride with a half-life of less than 1s at 39 °C below pH 3. The mechanism of catalysis, and the factors responsible for this extremely high reactivity, are discussed.

Nicotinic acid metabolism. V. A cobamide coenzyme-dependent conversion of alpha-methyleneglutaric acid to dimethylmaleic acid.

A new B(12)-coenzyme-dependent isomerization, catalyzed by extracts of a nicotinate-fermenting clostridium, results in the conversion of alpha-methyleneglutaric acid to dimethylmaleic acid. These two acids are intermediates in the multistep anaerobic process wherein nicotinate is converted, ultimately, to one mole each of propionate, acetate, carbon dioxide, and ammonia. Dimethylmaleic acid reacts in its anhydride form with 2,4-dinitrophenylhydrazine to form N-2',4'-dinitrophenyl-anilino-3,4-dimethylmaleimide. The characteristic reddish color exhibited by the latter derivative in alkaline solution serves as a convenient quantitative assay for dimethylmaleic acid. Comparison of the 2,4-dinitrophenylhydrazine derivatives of the product of the enzymic reaction and of synthetic dimethylmaleic anhydride showed them to be identical in every respect.

Reactions of acetylenes with noble-metal halides. VI. The reactions of 2-butyne with chlorodicarbonylrhodium dimer

Chlorodicarbonylrhodium dimer ([Rh(CO)2Cl]2) reacted with 2-butyne at 80° in benzene to give a mixture of compounds which contained hexamethylbenzene, duroquinone, chloro(π-duroquinone)-rhodium dimer, and chloro(π-tetramethylcyclopentadienone)rhodium. At 25° 2-butyne and [Rh(CO)2Cl]2 reacted to give a brown solid of variable composition (C), which could not be purified. Reaction of (C) with CO in methylene chloride gave a related solid (D) also of variable composition. Treatment of (C), or better (D), with an excess of triphenylphosphine gave chloro(dimethylmaleyl)bis(triphenylphosphine)-rhodium and (Ph3P)2RhCOCl. The former was identified by analysis, spectra, and its oxidation to dimethylmaleic anhydride. Reaction of (D) with p-toluidine gave chloro(dimethylmaleyl)carbonylbis(p-toluidine)rhodium, which on treatment with excess triphenylphosphine also gave chloro(dimethyl-maleyl)bis(triphenylphosphine)rhodium.

Liquid-phase photolysis. Part IX. exo-Photodimerisation of dimethylmaleic anhydride

The known photodimer of dimethylmaleic anhydride is shown, on chemical and crystallographic evidence, to have the trans structure.

Kinetics of the Hydrolysis and Formation of Dimethylmaleic Anhydride in Solvent Mixtures.

Kinetics of the Hydrolysis and Formation of Dimethylmaleic Anhydride in Solvent Mixtures.

The Action of Organometallic Compounds on Dimethylmaleic Anhydride

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe Action of Organometallic Compounds on Dimethylmaleic AnhydrideD. S. Tarbell and Clay WeaverCite this: J. Am. Chem. Soc. 1940, 62, 10, 2747–2750Publication Date (Print):October 1, 1940Publication History Published online1 May 2002Published inissue 1 October 1940https://doi.org/10.1021/ja01867a040RIGHTS & PERMISSIONSArticle Views40Altmetric-Citations2LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (438 KB) Get e-Alerts Get e-Alerts

Some Reactions of Maleic and Dimethylmaleic Anhydrides with Organometallic Compounds

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSome Reactions of Maleic and Dimethylmaleic Anhydrides with Organometallic CompoundsD. Stanley TarbellCite this: J. Am. Chem. Soc. 1938, 60, 1, 215–216Publication Date (Print):January 1, 1938Publication History Published online1 May 2002Published inissue 1 January 1938https://doi.org/10.1021/ja01268a504RIGHTS & PERMISSIONSArticle Views89Altmetric-Citations5LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (250 KB) Get e-Alerts Get e-Alerts