An Improved Reflection Colorimeter Integrated with a Coaxial Optical-fiber Cable for Highly Sensitive Solid-phase Colorimetry Using a Membrane Filter

Highly sensitive solid-phase colorimetry for nickel ion was demonstrated using an improved reflection colorimeter equipped with a coaxial optical-fiber cable. The nickel complex with α-furil dioxime was collected on a small-size membrane filter embedded in a disposable syringe filter unit. The leading edge of the optical-fiber cable was connected to the syringe filter unit via a Luer-lock fitting, and the color intensity of the sample on the filter was evaluated accurately. The detection limit was 0.8 ng in 2.5 mL of the complex solution (0.3 μg L−1). This improved configuration is applicable to highly sensitive on-site analysis without expensive instruments nor high laboratory skills

Ring-Mesh Model of Proteoglycan Glycosaminoglycan Chains in Tendon based on Three-dimensional Reconstruction by Focused Ion Beam Scanning Electron Microscopy

Tendons are composed of collagen fibrils and proteoglycan predominantly consisting of decorin. Decorin is located on the d-band of collagen fibrils, and its glycosaminoglycan (GAG) chains have been observed between collagen fibrils with transmission electron microscopy. GAG chains have been proposed to interact with each other or with collagen fibrils, but its three-dimensional organization remains unclear. In this report, we used focused ion beam scanning electron microscopy to examine the three-dimensional organization of the GAG chain in the Achilles tendon of mature rats embedded in epoxy resin after staining with Cupromeronic blue, which specifically stains GAG chains. We used 250 serial back-scattered electron images of longitudinal sections with a 10-nm interval for reconstruction. Three-dimensional images revealed that GAG chains form a ring mesh-like structure with each ring surrounding a collagen fibril at the d-band and fusing with adjacent rings to form the planar network. This ring mesh model of GAG chains suggests that more than two GAG chains may interact with each other around collagen fibrils, which could provide new insights into the roles of GAG chains