Info: 90 Caplets
Trophic Copper Chelazome is an excellent source of copper, as it's chelated with natural amino acids, so they can be absorbed by the intestines much better.
Info: 90 Caplets
Trophic Copper Chelazome is an excellent source of copper, as it's chelated with natural amino acids, so they can be absorbed by the intestines much better.
Product Notes:
Copper is an essential trace mineral found in every body tissue; it helps produce red blood cells and connective tissue; it works with iron to metabolize food into hemoglobin, which enables us to use oxygen; it can increase our ability to resist stress and disease, partly by working with enzymes, such as by catalyzing the antioxidant superoxide dismutase; it can even help prevent the loss of pigmentation in the hair and skin.
Ingredients:
Each caplet contains: 2 mg Copper (Bisglycinate) (Amino Acid Chelate).
Non-medicinal ingredients: Microcrystalline cellulose, dibasic calcium phosphate dihydrate, magnesium stearate.
Manufactured under the unique Albion Laboratories' process whereby the minerals are chelated by amino acids, peptides and polypeptides.
Suggested Usage:
Adults: take one caplet daily, or as recommended by a healthcare practitioner.
Warnings:
Do not use Trophic Copper Chelazome if you have a copper storage metabolism disorder, such as Wilson's disease.
Health Canada Natural Product Number: 00334049.
Supporting Science:
Chen, Ji et al. “The molecular mechanisms of copper metabolism and its roles in human diseases.” Pflugers Archiv: European Journal of Physiology, 2020.
Gombart, Adrian F et al. “A Review of Micronutrients and the Immune System-Working in Harmony to Reduce the Risk of Infection.” Nutrients, 2020
Guengerich, F Peter. “Introduction to Metals in Biology 2018: Copper homeostasis and utilization in redox enzymes.” The Journal of Biological Chemistry, 2018.
Myint, Zin W et al. “Copper deficiency anemia: review article.” Annals of Hematology, 2018.
Robinett, Natalie G et al. “Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains.” The Journal of Biological Chemistry, 2018.