Electron spin resonance (ESR) of tooth enamel is a recently developed method for the retrospective dose estimation of human radiation exposures. The assay requires isolation of enamel from dentin, which is difficult because the boundary between enamel and dentin is not easily discernible. Here we describe a simple method for isolating enamel by alkaline denaturation of dentin. The method requires 4 weeks, but scratching of the denatured and hence softened dentin is needed only once a week. Above all, no special skill is required. We found that the alkaline treatment did not cause deterioration of the ESR signal recorded in enamel exposed to 2 Gy of gamma rays prior to its isolation. The assay is particularly suited for teeth containing many cracks that were generated during long-term storage after extraction of the teeth. Such teeth tend to disintegrate during enamel isolation processes, which poses difficulties to isolate enamel mechanically from individual small pieces.
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http://dx.doi.org/10.1269/jrr.38.173 | DOI Listing |
Protein Expr Purif
January 2025
Department of Chemistry, Indian Institute of Technology, Delhi, India. Electronic address:
The aim of this study was to purify BMP-2 in an easy and time-efficient way. We have developed a new method in which BMP-2 is produced through leaky expression in E. coli BL21 (DE3) cells as inclusion bodies, eliminating the need for inducer Isopropyl β-D-1-thiogalactopyranoside (IPTG).
View Article and Find Full Text PDFJ Mass Spectrom
January 2025
Graduate School of Medical Life Science, Yokohama City University, Yokohama, Kanagawa, Japan.
In our previous work, the sodiation of melittin, cytochrome c, and ubiquitin in a 1 mM NaOH water/methanol solution was studied by electrospray mass spectrometry. It was suggested that the α-helix is more resistant to sodiation than the β-sheet. In this study, sodiation of enhanced green fluorescent protein (EGFP) composed of a β-barrel was studied in 1% CHCOOH (AcOH) or 1 mM NaOH water/methanol solution by electrospray mass spectrometry.
View Article and Find Full Text PDFJ Food Sci
December 2024
Department of Food Science, Cornell University, Ithaca, New York, USA.
This research investigated the effectiveness of supercritical fluid extrusion (SCFX) to modify the functional and structural characteristics of pea protein concentrate (PPC) and pea flour (PF). The results indicate that the SCFX process favorably modified the hydration properties of PPC and PF needed for developments in the structural and textural qualities of the meat analogs and other similar products. The water-holding capacity of extruded PPC and PF improved significantly.
View Article and Find Full Text PDFACS Appl Mater Interfaces
December 2024
Biological Physics Group, School of Physics and Astronomy, Faculty of Science and Engineering, The University of Manchester, Oxford Road, Manchester M13 9PL, United Kingdom.
Investigating the molecular conformations of monoclonal antibodies (mAbs) adsorbed at the solid/liquid interface is crucial for understanding mAb solution stability and advancing the development of mAb-based biosensors. This study examines the pH-dependent conformational plasticity of a human IgG1k mAb, COE-3, at the SiO/water interface under varying pH conditions (pH 5.5 and 9).
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Chemistry and Environmental Engineering, Shenzhen University, Shenzhen 518060, China; Shenzhen Key Laboratory of Food Nutrition and Health, Shenzhen University, Shenzhen 518060, China; Guangdong Engineering Technology Research Center of Aquatic Food Processing and Safety Control, Shenzhen University, Shenzhen 518060, China; Institute for Innovative Development of Food Industry, Shenzhen University, Shenzhen 518060, China. Electronic address:
In order to assess the potential of fractionated Schizochytrium sp. protein as functional proteins, the proteins were fractionally extracted. The structure, thermal characteristic and cross-linking interaction of proteins, along with the gel properties of heat-induced gels were analyzed and compared to those of albumin from chicken egg white (ACEW).
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