44 research outputs found
Corporate Social Responsibility (CSR) in Asia: a seven-country study of CSR web site reporting
This article addresses four hypotheses: (a) that corporate social responsibility (CSR) in Asia is not homogeneous but varies among countries, (b) that the variation is explained by stages of development, (c) that globalization enhances the adoption of CSR in Asia, and (d) that national business systems structure the profile of multinational corporations’ CSR. These hypotheses are investigated through analysis of Web site reporting of 50 companies in seven Asian countries: India, Indonesia, Malaysia, the Philippines, South Korea, Singapore, and Thailand. The article concludes that CSR does vary considerably among Asian countries but that this variation is not explained by development but by factors in the respective national business systems. It also concludes that multinational companies are more likely to adopt CSR than those operating solely in their home country but that the profile of their CSR tends to reflect the profile of the country of operation rather than the country of origin
Second Order Perturbations in the Randall-Sundrum Infinite Brane-World Model
We discuss the non-linear gravitational interactions in the Randall-Sundrum
single brane model. If we naively write down the 4-dimensional effective action
integrating over the fifth dimension with the aid of the decomposition with
respect to eigen modes of 4-dimensional d'Alembertian, the Kaluza-Klein mode
coupling seems to be ill-defined. We carefully analyze second order
perturbations of the gravitational field induced on the 3-brane under the
assumption of the static and axial-symmetric 5-dimensional metric. It is shown
that there remains no pathological feature in the Kaluza-Klein mode coupling
after the summation over all different mass modes. Furthermore, the leading
Kaluza-Klein corrections are shown to be sufficiently suppressed in comparison
with the leading order term which is obtained by the zero mode truncation. We
confirm that the 4-dimensional Einstein gravity is approximately recovered on
the 3-brane up to second order perturbations.Comment: 15 pages, 2 figures, comment and reference added, typos correcte
IMMUNOCHEMICAL PROPERTIES OF THYROID PROTEINS
Saline extracts obtained from both beef and hog thyroid glands were chromatographed on Sephadex G-200. An ultracentrifugal and immunochemical examination of the fractions showed that subfractions which possessed the 19 S component and a sufficient concentration of the 25 S component gave rise to two precipitin bands by the agar gel diffusion technique. Immunoelectrophoretic studies indicated that these antigens migrated in the region of α2globulins. In addition, it was found that subfractions which contained both the 19 S and 25 S components had higher extinction coefficients at 280 mμ and lower OD280/OD260ratios than those in which the 19 S component occurred alone. From these results, it can be suggested that the 19 S and 25 S components have different immunochemical and spectrophotometric properties.</jats:p
Effect of antigen stimulation on antigen-specific IgE-plaque-forming cells from peripheral-blood lymphocytes of atopics
A STUDY OF THE THYROID PROTEIN METABOLISM OF THE THIOURACIL-TREATED RAT
Oral administration of 2-thiouracil, for periods up to 28 days, greatly affected the soluble proteins of the rat thyroid gland. After 2 days, the iodine/protein ratio declined to less than half that present in the normal group. Ultracentrifugal analyses of the thyroid extracts showed a decrease in the 19 S thyroglobulin component, and a progressive increase in the 3 S component. After 7 days of treatment with 2-thiouracil, the 3 S component was the major protein constituent. The 11 S component rose to a maximum at 7 days and subsequently declined. Chromatographic fractionation of some of the thyroid extracts on Sephadex G-200 revealed similar changes in protein distributions. Both the whole thyroid extracts and their Sephadex G-200 fractions were examined by immunoelectrophoresis and the 19 S, 11 S, and 3 S components were characterized as having electrophoretic mobilities in the albumin-α1, α2, and α1-β regions respectively. By the micro-Ouchterlony agar gel technique, the 3 S component did not cross-react with the 19 S or 11 S components. In addition, the 19 S and (or) 11 S components of the 14-day group showed only partial cross-reaction with those of the normal group.</jats:p
THE PURIFICATION OF BEEF THYROGLOBULIN WITH THE USE OF GEL FILTRATION
A method is described for preparing a 19 S thyroglobulin component from a saline beef thyroid extract by chromatographic fractionation on Sephadex G-200. By employing Sephadex G-200 it was possible to separate a saline extract of minced beef thyroid gland into several fractions, the first of which (fraction I) contained approximately 60% of the protein and 96% of the iodine. Spectrophotometric, ultracentrifugal, and immunochemical methods revealed that fraction I possessed, in addition to the 19 S thyroglobulin protein, a 25 S component as well as serum proteins. A narrow band of fraction I appeared to be free of both the 25 S component and the serum proteins. The material in this subfraction had a sedimentation constant of S20,w = 19.1 and contained 1.2 mg of iodine per 100 mg of protein.</jats:p
THE PURIFICATION OF BEEF THYROGLOBULIN WITH THE USE OF GEL FILTRATION
A method is described for preparing a 19 S thyroglobulin component from a saline beef thyroid extract by chromatographic fractionation on Sephadex G-200. By employing Sephadex G-200 it was possible to separate a saline extract of minced beef thyroid gland into several fractions, the first of which (fraction I) contained approximately 60% of the protein and 96% of the iodine. Spectrophotometric, ultracentrifugal, and immunochemical methods revealed that fraction I possessed, in addition to the 19 S thyroglobulin protein, a 25 S component as well as serum proteins. A narrow band of fraction I appeared to be free of both the 25 S component and the serum proteins. The material in this subfraction had a sedimentation constant of S20,w = 19.1 and contained 1.2 mg of iodine per 100 mg of protein.</jats:p
