The rather complete data set of hadron yields from central Si + A collisions at the Brookhaven AGS is used to test whether the system at freeze-out is in thermal and hadro-chemical equilibrium. Rapidity and transverse momentum distributions are discussed with regards to the information they provide on hydrodynamic flow.The goal of the ultra-relativistic heavy-ion program at the BNL AGS and CERN SPS is to study highly excited and dense nuclear matter and possibly the transition from hot and dense hadronic matter to deconfined quark-matter with restored chiral symmetry. While future collider experiments will probe a hot quark-gluon plasma with low net baryon density, present fixed target experiments create matter, possibly quark-matter, at very high baryon density and moderate temperature.The present paper is following up on an earlier suggestion by some of us [1], based on the first AGS and SPS data, that a high degree of thermalization is reached and that there is evidence for hydrodynamic expansion of the created fireball. We now use the much larger set of data from central Si + A collisions at the AGS first to discuss quantitatively the 1
A novel human apolipoprotein designated apolipoprotein M (apoM) is described. The unique N-terminal amino acid sequence of apoM was found in an approximately 26-kDa protein present in a protein extract of triglyceride-rich lipoproteins (TGRLP). The isolated apoM cDNA (734 base pairs) encoded a 188-amino acid residue-long protein, distantly related to the lipocalin family. The mRNA of apoM was detected in the liver and kidney. Western blotting demonstrated apoM to be present in high density lipoprotein (HDL) and to a lesser extent in TGRLP and low density lipoproteins (LDL). The first 20 amino acid residues of apoM constituted a hydrophobic segment with characteristic features of a signal peptide. This was retained in the mature protein because of the lack of a signal peptidase cleavage site. In vitro translation in the presence of microsomes demonstrated translocation of apoM over the membrane and glycosylation but no signal peptide cleavage. The in vitro translated product remained associated with the microsomes after treatment with carbonate at pH 11, demonstrating that apoM is an integral protein. This finding suggests that apoM is linked to the single phospholipid layer of lipoproteins with a hydrophobic signal anchor. In conclusion, a novel human apolipoprotein, the function of which remains to be determined, is described.
Parity-odd domains, corresponding to non-trivial topological solutions of the QCD vacuum, might be created during relativistic heavy-ion collisions. These domains are predicted to lead to charge separation of quarks along the system's orbital momentum axis. We investigate a three particle azimuthal correlator which is a P even observable, but directly sensitive to the charge separation effect. We report measurements of charged hadrons near center-of-mass rapidity with this observable in Au+Au and Cu+Cu collisions at √ sNN =200 GeV using the STAR detector. A signal consistent with several expectations from the theory is detected. We discuss possible contributions from other effects that are not related to parity violation.
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