3,418 research outputs found

    Equality of multiplicity free skew characters

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    In this paper we show that two skew diagrams lambda/mu and alpha/beta can represent the same multiplicity free skew character [lambda/mu]=[alpha/beta] only in the the trivial cases when lambda/mu and alpha/beta are the same up to translation or rotation or if lambda=alpha is a staircase partition lambda=(l,l-1,...,2,1) and lambda/mu and alpha/beta are conjugate of each other.Comment: 16 pages, changes from v1 to v2: corrected the proof of Theorem 3.5 and some typos, changes from v2 to v3: minor layout change, enumeration changed, to appear in J. Algebraic Combi

    On principal hook length partitions and durfee sizes in skew characters

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    In this paper we construct for a given arbitrary skew diagram A all partitions nu with maximal principal hook lengths among all partitions with the character [nu] appearing in the skew character [A]. Furthermore we show that these are also partitions with minimal Durfee size. This we use to give the maximal Durfee size for [nu] appearing in [A] for the cases when A decays into two partitions and for some special cases of A. Also this gives conditions for two skew diagrams to represent the same skew character.Comment: 13 pages, minor changes from v1 to v2 as suggested by the referee, to appear in Annals. Com

    Mehanizam toksičnosti i detoksikacije organofosfornih spojeva s naglaskom na istraživanja u Hrvatskoj

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    This review comprises studies on the mechanisms of toxicity and detoxication of organophosphorus (OP) compounds done in Croatia in different research areas. One area is the synthesis of antidotes against OP poisoning and their in vivo testing in experimental animals. In vitro studies included in this review focus on the mechanisms of reversible inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), protection of cholinesterases from inhibition by OPs, and reactivation of phosphylated cholinesterases. The third area comprises distribution profiles of BChE and paraoxonase (PON) phenotypes in selected population groups and the detection of OPs and metabolites in humans. Finally, methods are described for the detection of OP compounds in human blood and other media by means of cholinesterase inhibitionPrikazana su istraživanja vođena u Hrvatskoj na različitim područjima mehanizma toksičnosti i detoksikacije organofosfornih (OP) spojeva. Jedno je područje sinteza antidota protiv otrovanja OP spojevima i testiranje in vivo antidota na eksperimentalnim životinjama. Istraživanja in vitro odnose se na mehanizam reverzibilne inhibicije acetilkolinesteraze (AChE) i buturilkolinesteraze (BChE), zaštitu kolinesteraza od inhibicije OP spojevima te reaktivaciju fosfiliranih kolinesteraza. Treće je područje distribucija fenotipova BChE i paraoksonaze (PON) u odabranim populacijama te detekcija OP spojeva i njihovih metabolita u ljudima. Na kraju su opisane metode detekcije OP spojeva u ljudskoj krvi i drugim medijima koje se osnivaju na inhibiciji kolinesteraza

    Inhibition of Cholinesterases by the Oximes P2AM and Toxogonin

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    The reversible inhibition of electric eel acetylcholinesterase (EC 3.1.1.7) by P2AM (2-(hydroxyimino)methyl-1-methyl-pyridinium chloride) and Toxogonin (1,1\u27-[oxybis(methylene)] bis(4-(hydroxyimino) methyl-pyridinium) dichloride) was studied using ac.etylthiocholine as substrate. Two techniques were applied for measuring acetylthiocholine hydrolysis, the conventional spectrophotometric and the stopped-flow (at 25 °c in 100 mM phosphate buffer pH = 7.4). The correlation between the degree of inhibition, and acetylthiocholine and oxime concentrations fits a theoretical model which postulates that the substrate and the inhibitor bind to two sites on the enzyme: the catalytic site and an allosteric, substrate-inhibition, site. The calculated dissociation constants for the two sites are: 0.13 and 0.76 mM for P2AM, and 0.16 and 2.0 mM for Toxogonin. The suggested model is an alternative to the hypothesis that two types of binding occur within the catalytic site. Horse serum cholinesterase and bovine erythrocyte acetylcholinesterase are also inhibited by P2AM and Toxogonin to about the same degree as the electric eel enzyme. Acetylthiocholine reacts with P2AM and Toxogonin; assuming that the reaction is bimolecular the corresponding rate constants are 13.4 and 22.4 M-1 min-

    Inhibition of Cholinesterases by the Oximes P2AM and Toxogonin

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    The reversible inhibition of electric eel acetylcholinesterase (EC 3.1.1.7) by P2AM (2-(hydroxyimino)methyl-1-methyl-pyridinium chloride) and Toxogonin (1,1\u27-[oxybis(methylene)] bis(4-(hydroxyimino) methyl-pyridinium) dichloride) was studied using ac.etylthiocholine as substrate. Two techniques were applied for measuring acetylthiocholine hydrolysis, the conventional spectrophotometric and the stopped-flow (at 25 °c in 100 mM phosphate buffer pH = 7.4). The correlation between the degree of inhibition, and acetylthiocholine and oxime concentrations fits a theoretical model which postulates that the substrate and the inhibitor bind to two sites on the enzyme: the catalytic site and an allosteric, substrate-inhibition, site. The calculated dissociation constants for the two sites are: 0.13 and 0.76 mM for P2AM, and 0.16 and 2.0 mM for Toxogonin. The suggested model is an alternative to the hypothesis that two types of binding occur within the catalytic site. Horse serum cholinesterase and bovine erythrocyte acetylcholinesterase are also inhibited by P2AM and Toxogonin to about the same degree as the electric eel enzyme. Acetylthiocholine reacts with P2AM and Toxogonin; assuming that the reaction is bimolecular the corresponding rate constants are 13.4 and 22.4 M-1 min-
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