Category: Iron

  • HFE H63D & VO2 max

    SMOKE EM IF YOU GOT EM The HFE H63D is a single-nucleotide polymorphism in the HFE gene (c.187C>G, rs1799945), which results in the substitution of a histidine for an aspartic acid at amino acid position 63 of the HFE protein (p.His63Asp). HFE participates in the regulation of iron absorption. Homozygous H63D variant can occasionally be the cause of hemochromatosis. It is also…

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  • Transferrin binding and PH

    Transferrin binding to transferrin receptors reduces its affinity for iron. Two pathways can occur once endocytosed–degradation or recycling pathways. The degradation pathway is where the dissociation of ferric ions from transferrin occurs from an early and late endosome. Iron can now be utilized for storage or incorporated into hemoglobin. The recycling pathway involves the recycling of…

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  • Ovotransferrin aka conalbumin

    Ovotransferrin aka conalbumin

    Ovotransferrin (conalbumin) is a glycoprotein of egg white albumen. Egg white albumen is composed of multiple proteins, of which ovotransferrin is the most heat reliable. It has a molecular weight of 76,000 daltons and contains about 700 amino acids. Ovotransferrin makes up approximately 13% of egg albumen (in contrast to ovalbumin, which comprises 54%). As a member of the transferrin and metalloproteinase family, ovotransferrin has been found to possess antibacterial…

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  • Saprolite

    Saprolite

    Saprolite is a chemically weathered rock. Saprolites form in the lower zones of soil profiles and represent deep weathering of the bedrock surface. In most outcrops, its color comes from ferric compounds. Deeply weathered profiles are widespread on the continental landmasses between latitudes 35°N and 35°S. Conditions for the formation of deeply weathered regolith include a topographically moderate relief flat enough to prevent erosion and to allow leaching of the products of chemical weathering. A second…

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  • Biomining or what I suspect “healthcare” (and much of the “food” industry) has been up to for a very, very long time

    Biomining or what I suspect “healthcare” (and much of the “food” industry) has been up to for a very, very long time

    Biomining is the technique of extracting metals from ores and other solid materials typically using prokaryotes, fungi or plants (phytoextraction also known as phytomining or biomining). These organisms secrete different organic compounds that chelate metals from the environment and bring it back to the cell where they are typically used to coordinate electrons. It was discovered in the mid 1900s that microorganisms…

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  • Cupronickel or copper-nickel (CuNi) is an alloy of copper that contains nickel and strengthening elements, such as iron and manganese

    Cupronickel or copper-nickel (CuNi) is an alloy of copper that contains nickel and strengthening elements, such as iron and manganese

    The copper content typically varies from 60 to 90 percent. (Monel is a nickel-copper alloy that contains a minimum of 52 percent nickel.) Despite its high copper content, cupronickel is silver in colour. Cupronickel is highly resistant to corrosion by salt water, and is therefore used for piping, heat exchangers and condensers in seawater systems, as well as for…

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  • Ferrochelatase catalyses the eighth and terminal step in the biosynthesis of heme, converting protoporphyrin IX into heme B

    Ferrochelatase catalyses the eighth and terminal step in the biosynthesis of heme, converting protoporphyrin IX into heme B

    Protoporphyrin ferrochelatase (EC 4.98.1.1, formerly EC 4.99.1.1, or ferrochelatase; systematic name protoheme ferro-lyase (protoporphyrin-forming)) is an enzyme encoded by the FECH gene in humans. Ferrochelatase catalyses the eighth and terminal step in the biosynthesis of heme, converting protoporphyrin IX into heme B. It catalyses the reaction: protoheme + 2 H+ = protoporphyrin + Fe2+ Function Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX in the heme biosynthesis…

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  • Transferrins

    Transferrins are not limited to only binding to iron but also to different metal ions.

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  • Ceruloplasmin carries more than 95% of the total copper in healthy human plasma and in addition plays a role in iron metabolism. It was first described in 1948.

    Ceruloplasmin carries more than 95% of the total copper in healthy human plasma and in addition plays a role in iron metabolism. It was first described in 1948.

    Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the CP gene. Ceruloplasmin is the major copper-carrying protein in the blood, and in addition plays a role in iron metabolism. It was first described in 1948. Another protein, hephaestin, is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism. Function Ceruloplasmin (CP) is an enzyme (EC 1.16.3.1) synthesized…

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  • Rose madder aka madder

    Rose madder (also known as madder) is a red paint made from the pigment madder lake, a traditional lake pigment extracted from the common madder plant Rubia tinctorum. Madder lake contains two organic red dyes: alizarin and purpurin. As a paint, it has been described as a fugitive, transparent, nonstaining, mid valued, moderately dull violet red pigment in tints and medium solutions, darkening to an impermanent, dull magenta red in masstone. History Madder…

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  • Tryptophan tryptophylquinone (TTQ) formation

    Tryptophan tryptophylquinone (TTQ) is an enzyme cofactor, generated by posttranslational modification of amino acids within the protein. Methylamine dehydrogenase (MADH), an amine dehydrogenase, requires TTQ for its catalytic function. From Wikipedia where this page was last updated June 22, 2022 See also Amicyanin is a type I copper protein that plays an integral role in electron transfer. In bacteria such as Paracoccus denitrificans, amicyanin is part of a three-member redox complex, along…

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