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Color in Metals and Semiconductors
Published in Mary Anne White, Physical Properties of Materials, 2018
The blood of invertebrates in the phyla Arthropoda and Mollusca (e.g., crab, crayfish, lobster, snail, slug, octopus) contains hemocyanin as its oxygen carrier. Hemocyanin contains copper, which is bound directly to a protein. The oxygenated form, oxy-hemocyanin, contains bound oxygen, and this species absorbs light. There are three regions of maximum absorbance: one at a wavelength of 280 nm (due to the protein), and two others due to the copper one at 346 nm and one at 580 nm.
Animal biotechnology
Published in Firdos Alam Khan, Biotechnology Fundamentals, 2018
Despite its name, it is more closely related to spiders, ticks, and scorpions than to crabs. Horseshoe crabs are most commonly found in the Gulf of Mexico and along the northern Atlantic coast of North America. A main area of annual migration is Delaware Bay, although stray individuals are occasionally found in Europe. The blood of horseshoe crabs as well as that of most mollusks, including cephalopods and gastropods, contains the copper-containing protein hemocyanin at concentrations of about 50 g/L. These creatures do not have hemoglobin (iron-containing protein), which is the basis of oxygen transport in vertebrates. Hemocyanin is colorless when deoxygenated and dark blue when oxygenated. The blood in the circulation of these creatures, which generally live in cold environments with low oxygen tensions, is gray-white to pale yellow, and it turns dark blue when exposed to the oxygen in the air, as seen when they bleed.
Oxygenation of copper(I) complexes containing fluorine tagged tripodal tetradentate chelates: significant ligand electronic effects
Published in Journal of Coordination Chemistry, 2022
Runzi Li, Firoz Shah Tuglak Khan, Marcos Tapia, Shabnam Hematian
The dioxygen (O2) chemistry of synthetic copper(I) complexes and the oxidative properties of the resulting copper-O2 adducts are of importance due to their potential relevance to copper-containing proteins vital for aerobic life as well as their applications in chemical catalysis [1–5]. In nature, copper-dioxygen interactions are essential for facilitating an array of biological functions in many proteins including the dioxygen-carrier hemocyanin, monooxygenases where O2 is activated such as in tyrosinase, dopamine β-hydroxylase, and phenylalanine hydroxylase, or oxidases where O2 is reduced to H2O or H2O2 including in laccase, galactose oxidase, ascorbate oxidase, amine oxidase, and the heme-copper binuclear active site of cytochrome c oxidase [2,6–8].
Preparation monoclonal β-type anti-idiotype antibody of zearalenone and development of green ELISA quantitative detecting technique
Published in Preparative Biochemistry & Biotechnology, 2020
Luhuai Shi, Tao Yu, Miner Luo, Hong Wang
ZEN standard substance, β-zearalenol, α-zearalanol, β-zearalanol, zearalanone, Dexynivalenol, Fumonisin B1, Ochratoxin A, T2 toxin, HRP-labeled streptavidin biotin, HRP-conjugated goat anti-mouse IgG antibody (Fc specific or F(ab)’2 specific), Polyethylene glycol, Freund’s incomplete adjuvant, Freund’s complete adjuvant, TMB(3,3′,5,5′-Tetramethylbenzidine), hypoxanthine‐aminopterin‐thymidine (HAT), HT (HT Media Supplement), mouse monoclonal antibody subclass identification kit and PEG4000 were purchased from Sigma Co., Ltd. (USA). Quick adjuvant was purchased from Unique Biotechnology Co., Ltd. (Beijing, China). Immobilized pepsin, biotin labeling kit, Keyhole Limpet Hemocyanin (KLH) and BCA™ protein kit were purchased from Thermo Co., Ltd. (USA). Cell culture medium RPMI-1640, calf serum and hybridoma growth factor were purchased from PPA Co., Ltd (Austria). Myeloma cells SP2/0 were purchased from Shanghai Cell Biology (Shanghai, China). Anti-Ractopamine mAb, anti-Plumbum mAb, anti-Chrome mAb or anti-shrimp allergen mAb were purchased from Biolab Co. Ltd (Beijing, China). A kind of hybridoma secreting anti-ZEN monoclonal antibodies (1G4) was made in our lab. BALB/C mice were purchased from the experimental animal center of Southern Medical University Guangzhou, China. Other reagents were of analytical grade.
The concentration of Cu and Pb in the funnel spider Eratigena atrica (C. L. Koch 1843) (Araneae: Agelenidae) and its web
Published in Chemistry and Ecology, 2019
Justyna Rybak, Wioletta Rogula-Kozłowska, Krzysztof Loska, Kamila Widziewicz, Radosław Rutkowski
In our study the concentration level of Cu in spider bodies was ca. from 2 to 7 folds higher than those of Pb. In spiders, copper is necessary for the synthesis of oxygen-transporting Cu-containing hemocyanin. This may explain the different way of accumulation of both studied elements. Although the reaction of different arthropods to elevated Cu concentrations varies widely [17], this essential metal at low concentrations is known to be one of the most toxic elements [18]. For example, its compounds were used as pesticides which were found harmful to invertebrates. Babczyńska et al. [3] found that two metals: essential Cu and toxic Cd were processed by spiders Agelena labyrinthica (Agelenidae) in two different ways. The excess of Cu was eliminated from the body, in contrast to toxic Cd which was concentrated in spiders.