Universal scaling of strange particle pTp_{\rm T} spectra in pp collisions

As a complementary study to that performed on the transverse momentum ($p_{\rm T}$) spectra of charged pions, kaons and protons in proton-proton (pp) collisions at LHC energies 0.9, 2.76 and 7 TeV, we present a scaling behaviour in the $p_{\rm T}$ spectra of strange particles ($K_{S}^{0}$, $\rm \Lambda$, $\rm \Xi$ and $\phi$) at these three energies. This scaling behaviour is exhibited when the spectra are expressed in a suitable scaling variable $z=p_{\rm T}/K$, where the scaling parameter $K$ is determined by the quality factor method and increases with the center of mass energy ($\sqrt{s}$). The rates at which $K$ increases with $\mathrm{ln}\sqrt{s}$ for these strange particles are found to be identical within errors. In the framework of the colour string percolation model, we argue that these strange particles are produced through the decay of clusters that are formed by the colour strings overlapping. We observe that the strange mesons and baryons are produced from clusters with different size distributions, while the strange mesons (baryons) $K_{S}^{0}$ and $\phi$ ($\rm \Lambda$ and $\rm \Xi$) originate from clusters with the same size distributions. The cluster's size distributions for strange mesons are more dispersed than those for strange baryons. The scaling behaviour of the $p_{\rm T}$ spectra for these strange particles can be explained by the colour string percolation model in a quantitative way.Comment: 8 pages, 10 figures, accepted by EPJ

High Activity Mutants of Butyrylcholinesterase for Cocaine Hydrolysis

Butyrylcholinesterase (BChE) polypeptide variants of the presently-disclosed subject matter have enhanced catalytic efficiency for (-)-cocaine, as compared to wild-type BChE. Pharmaceutical compositions of the presently-disclosed subject matter include a BChE polypeptide variant having an enhanced catalytic efficiency for (-)-cocaine. A method of the presently-disclosed subject matter for treating a cocaine-induced condition includes administering to an individual an effective amount of a BChE polypeptide variant, as disclosed herein, to lower blood cocaine concentration

High Activity Mutants of Butyrylcholinesterase for Cocaine Hydrolysis

Butyrylcholinesterase (BChE) polypeptide variants of the presently-disclosed subject matter have enhanced catalytic efficiency for (−)-cocaine, as compared to wild-type BChE. Pharmaceutical compositions of the presently-disclosed subject matter include a BChE polypeptide variant having an enhanced catalytic efficiency for (−)-cocaine. A method of the presently-disclosed subject matter for treating a cocaine-induced condition includes administering to an individual an effective amount of a BChE polypeptide variant, as disclosed herein, to lower blood cocaine concentration

High Activity Mutants of Butyrylcholinesterase for Cocaine Hydrolysis

Butyrylcholinesterase (BChE) polypeptide variants of the presently-disclosed subject matter have enhanced catalytic efficiency for (−)-cocaine, as compared to wild-type BChE. Pharmaceutical compositions of the presently-disclosed subject matter include a BChE polypeptide variant having an enhanced catalytic efficiency for (−)-cocaine. A method of the presently-disclosed subject matter for treating a cocaine-induced condition includes administering to an individual an effective amount of a BChE polypeptide variant, as disclosed herein, to lower blood cocaine concentration