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  2. Antimicrobial properties of copper - Wikipedia

    en.wikipedia.org/wiki/Antimicrobial_properties...

    Copper alloy surfaces have intrinsic properties that destroy many microorganisms.In the interest of protecting public health, especially in healthcare environments with their susceptible patient populations, an abundance of peer-reviewed antimicrobial efficacy studies have been conducted in the past ten years regarding copper's efficacy to destroy E. coli O157:H7, methicillin-resistant ...

  3. Copper in biology - Wikipedia

    en.wikipedia.org/wiki/Copper_in_biology

    Copper deficiency and toxicity can be either of genetic or non-genetic origin. [8] The study of copper's genetic diseases, which are the focus of intense international research activity, has shed insight into how human bodies use copper, and why it is important as an essential micronutrient. [9]

  4. Copper peptide GHK-Cu - Wikipedia

    en.wikipedia.org/wiki/Copper_peptide_GHK-Cu

    Copper is required for iron metabolism, oxygenation, neurotransmission, embryonic development and many other essential biological processes. Another function of copper is signaling – for example, stem cells require a certain level of copper in the media to start their differentiation into cells needed for repair. Thus, GHK-Cu's ability to ...

  5. Copper - Wikipedia

    en.wikipedia.org/wiki/Copper

    Copper is sometimes used in decorative art, both in its elemental metal form and in compounds as pigments. Copper compounds are used as bacteriostatic agents, fungicides, and wood preservatives. Copper is essential to all living organisms as a trace dietary mineral because it is a key constituent of the respiratory enzyme complex cytochrome c ...

  6. Hemocyanin - Wikipedia

    en.wikipedia.org/wiki/Hemocyanin

    Phenoloxidase are copper containing tyrosinases. These proteins are involved in the process of sclerotization of arthropod cuticle, in wound healing, and humoral immune defense. Phenoloxidase is synthesized by zymogens and are activated by cleaving an N-terminal peptide. [7] Hexamerins are storage proteins commonly found in insects.

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