Tag: Hemoglobin

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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September 19, 2024
Isoleucine, Tryptophol, Sleeping Sickness, The Disulfiram Effect and One Trick Hypnotists From Hell

Isoleucine (symbol Ile or I) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH+3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a hydrocarbon side chain with a branch (a central carbon atom bound to three other carbon atoms). It is classified as a non-polar, uncharged (at physiological pH), branched-chain, aliphatic amino acid. It…
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January 6, 2024
Tetramers and tetrameric protein

A tetramer is an oligomer formed from four monomers or subunits. The associated property is called tetramery. An example from inorganic chemistry is titanium methoxide with the empirical formula Ti(OCH3)4, which is tetrameric in solid state and has the molecular formula Ti4(OCH3)16. An example from organic chemistry is kobophenol A, a substance that is formed by combining four molecules of resveratrol. In biochemistry, it similarly refers to a biomolecule formed of four units, that are the…
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January 6, 2024