ABSTRACT
The shear viscosity to entropy ratio (eta/s) is estimated for the hot and dense QCD matter created in Au+Au collisions at BNL Relativistic Heavy Ion Collider (square root[s_{NN}]=200 GeV). A very low value is found; eta/s approximately 0.1, which is close to the conjectured lower bound (1/4pi). It is argued that such a low value is indicative of thermodynamic trajectories for the decaying matter which lie close to the QCD critical end point.
ABSTRACT
The yield for the multistrange Xi(-) hyperon has been measured in 6A GeV Au+Au collisions via reconstruction of its decay products pi(-) and Lambda, the latter also being reconstructed from its daughter tracks of pi(-) and p. The measurement is rather close to the threshold for Xi(-) production and therefore provides an important test of model predictions. The measured yield for Xi(-) and Lambda are compared for several centralities. In central collisions the Xi(-) yield is found to be in excellent agreement with statistical and transport model predictions, suggesting that multistrange hadron production approaches chemical equilibrium in high baryon density nuclear matter.
ABSTRACT
Source images are extracted from two-particle correlations constructed from strange and nonstrange hadrons produced in 6A GeV Au+Au collisions. Very different source images result from pp vs p Lambda vs pi(-)pi(-) correlations. Scaling by transverse mass can describe the apparent source size ratio for p/pi(-) but not for Lambda/pi(-) or Lambda/p. These observations suggest important differences in the space-time emission histories for protons, pions, and neutral strange baryons produced in the same events.
ABSTRACT
The N,N-dimethylformamide-hydrolyzing enzyme (DMFase) from Pseudomonas DMF 3/3 has been purified to apparent electrophoretic homogeneity with an overall 49-fold purification, a 24% yield and a final specific activity of 1.98 mumol N,N-dimethylformamide (DMF) hydrolyzed min-1 (mg protein)-1. The native DMFase has a relative molecular mass of 250 000 and is composed of two light-chain (Mr = 15 000) and two heavy-chain (Mr = 105 000) subunits. The stability of DMFase is optimal at pH values above 7.5 and at temperatures below 20 degrees C. The activity of the enzyme is inhibited by metal-chelating agents such as EDTA and 2,2'-dipyridyl. Emission and atomic absorption spectroscopy measurements showed that iron is present in significant amounts in DMFase, indicating that it is an iron-containing amidohydrolase. In the ultraviolet/visible spectrum prominent bands were observed at 224 nm, 280 nm and 396 nm and shoulders are present at 418 nm and 467 nm. DMFase from Ps. DMF 3/3 has an isoelectric point of 7.7. The enzyme exhibits optimal activity between pH 5 and 6 and at 40 degrees C. The substrate spectrum is rather narrow. The enzyme hydrolyzes preferentially substituted short-chain aliphatic amides such as DMF, N-ethylformamide and N-methylformamide. N,N-dimethylformamide, N,N-dimethylacetamide and unsubstituted amides, e.g. formamide, prolinamide, acetamide, acrylamide and butyramide are substrates as well, but are hydrolysed at significantly lower rates. DMFase obeys Michaelis-Menten kinetics and its Km and Vmax values for DMF are 13.8 mM and 1.89 U/mg, respectively, as determined from a Lineweaver-Burk plot.
