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In the literature to date, there are no studies that directly evaluate microscopic urine examination results obtained by a physician compared to those of a trained laboratory technician. Our purpose in undertaking this study was to determine whether there would be comparable results obtained by these two groups. The study took place in an Emergency Medicine Department with 45,000 visits annually. Each urine sample obtained on patients presenting to the Emergency Department was divided into two lots: one was sent to the laboratory and the other was analyzed by the emergency physician. A comparison of both dipstick and microscopic results by physician and laboratory staff was then made using sensitivity, specificity, and Kappa analysis. Statistical analysis of the data revealed close agreement between the emergency physician and laboratory technician with respect to the following components of urinalysis: red blood cell urinalysis and microscopy, leukocyte esterase, and nitrite testing. Microscopy for white cells and bacteria and testing for proteinuria were not in close agreement. Urinalysis by emergency physicians is comparable to laboratory technicians for a number of the testing components. However, in this limited pilot study, emergency physicians were not able to consistently perform urinalysis for the laboratory standard.

Summary Soybean leucyl-tRNAs and synthetases were localized in cytoplasm, mitochondria and chloroplasts. Total leucyl-tRNA synthetase (cytoplasmic) resolves into three enzyme peaks when chromatographed on hydroxylapatite columns (HA) while mitochondrial and chloroplastic enzymes result in one peak each. Cytoplasmic enzyme peak 1 preferentially charges cytoplasmic tRNAleu species 5 and 6 and chloroplastic tRNAleu species 5 and 6. Cytoplasmic enzyme peak 2 preferentially charges cytoplasmic or mitochondrial tRNAleu species 1—4. Similarly, cytoplasmic enzyme peak 3 preferentially charges cytoplasmic or mitochondrial tRNAleu species 1—4. Chloroplast enzyme acylates only two tRNAleu species 5 and 6 of chloroplast tRNA and preferentially charges peaks 5 and 6 of total cytoplasmic tRNA. Mitochondrial enzyme acylates four mitochondrial tRNAleu species 1—4 and the same four cytoplasmic tRNAleu species 1—4. However, the acylation of tRNAleu species 3 and 4 using mitochondrial tRNA is considerably increased. E. coli tRNA, charged with homologous synthetase and separated on RPC-5 column yields five tRNAleu species. Cytoplasmic enzyme (crude) acylates all five tRNAleu species of E. coli. Cytoplasmic enzyme 1 from HA column or purified chloroplastic enzymes acylate all five tRNAleu species of E. coli whereas cytoplasmic enzyme 2 and 3 and/or purified mitochondrial enzyme preferentially acylate tRNAleu species 1 and 2 of E. coli.

The reaction of arsenic trifluoride with a m-xylene solution of cyclopentadienyliron dicarbonyl dimer contained in a Pyrex-glass vessel has unexpectedly produced the tetrafluoroborate salt of the highly unusual [Fe3(h5-C5H5)3(CO)5As4O5]+ monocation. An X-ray diffraction analysis has elucidated unequivocally both the stoichiometry and atomic arrangement of this compound in complete harmony with its physical and chemical properties. The diamagnetic monocation may be envisioned as arising from the cubic Ta bird-cage As4O6 molecule through the replacement of one of its six edge-bridged oxygen atoms with an iron-bridged [Fe(h5-C5H5)(CO)]+ species together with the concomitant addition of a terminal one-electron donating [Fe(h5-C5H5)(CO)2] ligand to each of the two iron-bridged arsenic atoms in order for them to maintain a closed-shell electronic configuration The resulting [As4O5Fe] core closely conforms to C2v-2mm symmetry, while the entire monocation has an approximate mirror plane. A salient structural feature is that there is no appreciable structural influence on the As4O6 architecture due to this formal transmutation into the monocation other than an increase of 0.06 A along the iron-bridged edge of the nonbonded tetrahedron of arsenic atoms. The orange-red compound crystallizes with four monocations and four BF4- anions in a monoclinic unit cell of P21/c symmetry with a = 15.571(3), b = 14.800(3), c = 15.389(3) A, and β = 126.176(6)°. The crystal structure has been refined to a final unweighted R1 value of 4.5% for 2400 independent diffractometry-collected data with I ⩾ 2.0 σ(I).