Search

To determine whether high-sensitivity C-reactive protein (hsCRP) and serum amyloid A (SAA) predict stroke, vascular events, and mortality in a prospective cohort study.

A domain-extension method for quantitative detection of irregular-shape cavities inside irregular-shape bodies is presented. An auxiliary problem is introduced in the solution of the cavities. In the auxiliary problem, the original body domain at the cavity side is extended so that the original cavity walls become interior points. The position of the cavities can then be found by solving the temperature field in the extended domain and matching the temperatures and heat fluxes at the interior points to the conditions imposed on the cavities. A boundary-element method is used for the solution of the auxiliary problem, and by means of four examples, the accuracy of the domain extension method is established. The paper provides the details for the numerical solution of the cavities. Limitation of the method in the detection of multiple cavities is also explored. The domain-extension method has shown to be highly effective in quantitative detection of cavities in single-cavity bodies.

Two glutathione S-transferase fusion proteins containing 44 (p1503) and 75 (p1509) amino acid residues of the rubella virus E1 glycoprotein were expressed in Escherichia coli with the aim of producing a recombinant rubella virus antigen for use in serological assays. p1503 contained three neutralizing and hemagglutinating epitopes (G. M. Terry, L. M. Ho-Terry, P. Londesborough, and K. R. Rees, Arch. Virol. 98:189-197, 1988); p1509 contained the putative neutralization domain described by Mitchell et al. (L. A. Mitchell, T. Zhang, M. Ho, D. Decarie, A. Tingle, M. Zrein, and M. Lacroix, J. Clin. Microbiol. 30:1841-1847, 1992) in addition to the three epitopes present in p1503. Both fusion proteins were soluble and affinity purified on glutathione-Sepharose 4B. In Western blots (immunoblots), p1503 and p1509 reacted with human sera containing rubella virus-specific immunoglobulin G. When used as antigens in indirect enzyme immunoassays to detect rubella virus-specific immunoglobulin G, p1503 correctly identified the rubella virus antibody status of 43 (76.8%) and p1509 correctly identified that of 48 (85.7%) of 56 serum samples received for routine rubella virus antibody screening. The results obtained with p1509 compare well with those obtained with a latex agglutination assay.

The present work is an attempt to develop a new method to determine sex from the skull with lateral radiographic cephalometry and discriminant function analysis. The superciliary ridges, frontal sinuses, external occipital protuberance, and mastoid processes were adopted as objects of lateral radiographic cephalometric measurements. With discriminant functions created from 18 established cephalometric variables, a total of 100 cases were classified into two sexual groups with 100% accuracy in a random sample of Taiwanese adults. Therefore, we may obtain a much greater reliability of sex determination from skulls according to this newly developed technique.

The phase composition and microstructure formation mechanism of in-situ Cu-Fe micro-composites were investigated. The microstructures of longitudinal and transverse sections were analyzed by light microscopy and scanning electron microscopy. The phase analysis was executed by X-ray diffraction. The common microstructure characteristic of Cu-XFe (X = 11, 14 and 17) alloys was that the second phase a-Fe dendrites were uniformly distributed in the Cu matrix. The disorderly distributed Fe dendrites of Cu-14Fe alloy underwent initial inhomogeneous deformation and then were gradually changed into the directionally arranged Fe fibers of in-situ Cu-14Fe micro-composite in the longitudinal section, and were gradually transformed into the irregular V-shaped Fe fibers in the transverse section. The initial inhomogeneous deformation and the irregular V-shaped Fe fibers in the transverse section are closely related to the formation of <110> texture.

ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.