Visible transmission spectroscopy for the assessment of egg freshness

The objective of this research was to investigate the feasibility of visible transmission spectroscopy for the non‐destructive assessment of the freshness of an individual egg. A total of 600 intact white‐shelled eggs of the same flock (Lohmann, 40 weeks of age) were measured. To obtain a considerable variation in freshness, groups consisting of 60 eggs were stored (18 °C, 55% RH) for 0, 2, 4, 6, 8, 10, 12, 14, 16 and 18 days. The non‐destructive spectral measurements were compared with the two most widely used destructive freshness parameters, namely Haugh units and albumen pH. A partial least squares (PLS1) model was built in order to predict Haugh units and pH of the albumen based on the transmission spectra. The correlation coefficients between the predicted value and the measured value were 0.842 and 0.867 for Haugh unit and pH of the albumen, respectively. These results show that the light transmission spectrum of an egg provides quantitative information about egg freshness. Relevant information concerning egg freshness is restricted to the interval between 570 and 750 nm. Furthermore, the models obtained for both destructive parameters were strikingly similar, indicating that Haugh unit and pH have the same physico‐chemical background. Copyright © 2006 Society of Chemical Industry     

The pharmacokinetics and protein-binding of fusidic acid in patients with severe renal failure requiring either haemodialysis or continuous ambulatory peritoneal dialysis

Antibiotic treatment options for Burkholderia cepacia infection are limited because of high intrinsic resistance. The problem is complicated by development of cross-resistance between antibiotics of different classes. We isolated antibiotic-resistant mutants by stepwise exposure to chloramphenicol (Chlor) and to trimethoprim/sulphamethoxazole (T/S) for four B. cepacia strains: ATCC13945, Per (clinical isolate), Cas and D4 (environmental isolates). Chlor(r) mutants did not produce chloramphenicol acetyl-transferase. Cross-resistance, defined as greater than four-fold increase in MIC by microtitre dilution method, was consistently seen in both types of mutants. For chloramphenicol-resistant (Chlor[r]) and trimethoprim/sulphamethoxazole-resistant (Tr/Sr) mutants of B. cepacia ATCC13945 and Cas, no MIC change was seen for piperacillin, ceftazidime, rifampicin, gentamicin, tobramycin, polymyxin B or azithromycin. B. cepacia-Per and -D4 mutants showed cross-resistance to ceftazidime and to piperacillin. Comparison of outer membrane protein (OMP) profiles of B. cepacia and their mutants by SDS-PAGE revealed Tr/Sr) mutants to be deficient in a major OMP (molecular weight 39-47 kDa). Tr/Sr mutants also expressed additional OMPs not found in wild type strains at 75-77 kDa for B. cepacia-ATCC13945 and -Cas, and 20-21 kDa in B. cepacia-D4 and -Per. No OMP changes occurred in Chlor(r) mutants. Lipopolysaccharide (LPS) profiles of each type of mutant showed new high and low molecular weight LPS bands. Cross-resistance seems to be mediated by alterations in porin and LPS for Tr/Sr mutants, but only by LPS in Chlor(r) mutants.     

Schwingfestigkeit von Schraube‐Mutter‐Verbindungen

High cycle fatigue of bolted connections Extensive tests regarding the influences on the fatigue of bolt‐nut‐connections of preloading with torsion, of preloading with yielding, of loading with superimposed bending and of the tested lot are processed. These influences are not yet known according to VDI 2230. New testing devices were designed for these tests, which allow a far less expensive operation and may easily be used for bolts of diameters up to M100 and testing frequencies up to 1000 Hz. The validity of fatigue resistance according to VDI 2230 is specified with respect to the test results. The determined influence of the tested lots is unexpectedly high. The manufacturing process of bolts should be improved to minimize this influence.     

Substrate-induced conformational change in a trimeric ornithine transcarbamoylase

The crystal structure of Escherichia coli ornithine transcarbamoylase (OTCase, EC 2.1.3.3) complexed with the bisubstrate analog N-(phosphonacetyl)-L-ornithine (PALO) has been determined at 2.8-A resolution. This research on the structure of a transcarbamoylase catalytic trimer with a substrate analog bound provides new insights into the linkages between substrate binding, protein-protein interactions, and conformational change. The structure was solved by molecular replacement with the Pseudomonas aeruginosa catabolic OTCase catalytic trimer (Villeret, V., Tricot, C., Stalon, V. & Dideberg, O. (1995) Proc. Natl. Acad. Sci. USA 92, 10762-10766; Protein Data Bank reference pdb 1otc) as the model and refined to a crystallographic R value of 21.3%. Each polypeptide chain folds into two domains, a carbamoyl phosphate binding domain and an L-ornithine binding domain. The bound inhibitor interacts with the side chains and/or backbone atoms of Lys-53, Ser-55, Thr-56, Arg-57, Thr-58, Arg-106, His-133, Asn-167, Asp-231, Met-236, Leu-274, Arg-319 as well as Gln-82 and Lys-86 from an adjacent chain. Comparison with the unligated P. aeruginosa catabolic OTCase structure indicates that binding of the substrate analog results in closure of the two domains of each chain. As in E. coli aspartate transcarbamoylase, the 240s loop undergoes the largest conformational change upon substrate binding. The clinical implications for human OTCase deficiency are discussed.     

Energy-dependent phase-shift analysis of 2H+4He scattering in the energy range 0.87

VM Krasnopol''sky  VI Kukulin  EV Kuznetsova  J Horáek  NM Queen 《Canadian Metallurgical Quarterly》1991,43(2):822-834