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This study was conducted using a hedonic pricing model to evaluate consumer preference for packaging and contents in five Asian countries: Japan, Indonesia, Singapore, Taiwan, and China. Results revealed that the marginal rate of substitution (MRS) of packaging for contents differs significantly among countries: 17.7 for Singapore, 8.58 for China, 2.71 for Taiwan, 1.65 for Japan and not significant for Indonesia. Share of Willingness-to-pay (WTP) for packaging accounted for 52.8% of the WTP for sales unit of a representative product in Japan and 46.2% in Taiwan, which were significantly higher than the results for Singapore (32.6%) and China (18.2%). Results showed that the higher the share of packaging in the WTP for a product, the higher the relative packaging weight per unit weight of contents. These results suggest that the relative demand for packaging to contents differs among countries. The results underscore the necessity of choosing suitable policy instruments and marketing strategies for different countries. [ABSTRACT FROM AUTHOR]

Human serum amyloid A (SAA) is a precursor protein involved in AA amyloidosis. The N-terminal region of the SAA molecule is crucial for amyloid fibril formation, and therefore modifications in this region are considered to influence the pathogenesis of AA amyloidosis. In the present study, using the N-terminal peptide corresponding to the putative first helix region of the SAA molecule, we investigated the influences of N-terminal modifications on amyloid fibril formation. Spectroscopic analyses revealed that carbamoylation of the N-terminal amino group delayed the onset of amyloid fibril formation. From transmission electron microscopic observations, the N-terminal carbamoylated aggregate showed remarkably different morphologies from the unmodified control. In contrast, acetylation of the N-terminal amino group or truncation of N-terminal amino acid(s) considerably diminished amyloidogenic properties. Furthermore, we also tested the cell toxicity of each peptide aggregate on cultured cells by two cytotoxic assays. Irrespective of carbamoylation or acetylation, MTT assay revealed that SAA peptides reduced the reductive activity of MTT on cells, whereas no apparent increase in LDH release was observed during an LDH assay. In contrast, N-terminal truncation did not affect either MTT reduction or LDH release. These results suggest that N-terminal modification of SAA molecules can act as a switch to regulate susceptibility to AA amyloidosis. [Display omitted] • How the N-terminal modifications of SAA affect amyloid formation was investigated. • Carbamoylation of the N-terminal amino group retarded the onset of amyloid formation. • N-terminal carbamoylation also affected the morphology of aggregates. • Acetylation or truncation considerably diminished the amyloidogenic properties. • N-terminal modifications of SAA can control the susceptibility to AA amyloidosis. [ABSTRACT FROM AUTHOR]