Taurine
Sulfoxide
Sulfonyl
Methane
Dimethyl
Methyl
Methylene (Blue)
Carotenoid (Red)

Methylene Blue
Thioninium
Thionine
Taurine
Amine
Amino
Phenol
Thiazine
Phenothiazine

A triglyceride is formed when three fatty acid molecules are attached to a glycerol molecule. Fatty acids are long hydrocarbon chains with a carboxylic acid group (COOH) at one end and a methyl group (CH3).

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Methylsulfonylmethane: Applications and Safety of a Novel Dietary Supplement

https://pmc.ncbi.nlm.nih.gov/articles/PMC5372953/

MSM has long been thought of as a sulfur donor for sulfur containing compounds such as methionine, cysteine, homocysteine, taurine.

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Polyphosphate and Fibrin Structure:

Polyphosphate, a chain of phosphate molecules, significantly affects fibrin clot structure.It enhances the structure of fibrin clots, making them more resistant to breakdown.

Polyphosphate released from activated platelets or microorganisms may modulate fibrin clot structure and increase its resistance to breakdown (fibrinolysis).

Plasmin, an enzyme involved in fibrinolysis, is essential for clearing fibrin from the fracture site.

Fibrinogen, the precursor of fibrin, can be phosphorylated, impacting its clotting and fibrinolytic properties.

Phosphorylation affects fibrin fiber thickness and how fibrinogen interacts with plasmin.

Fibrin can bind calcium phosphate and potentially promote mineralization.

Fibrin deposition, particularly in the absence of adequate plasmin activity, can contribute to heterotopic ossification (abnormal bone formation in soft tissues).

Plasmin, a key enzyme in fibrinolysis (the breakdown of blood clots), is a protein molecule and, as such, contains nitrogen atoms as part of its amino acid structure.

Plasmin's structure is held together by disulfide bonds, which are formed between sulfur atoms in cysteine residues within the protein.

Plasminogen (precursor to plasmin) contains 24 disulfide bridges.

Plasmin is a two-chain molecule formed from plasminogen activation, and the two chains are linked by disulfide bonds.

The kringle domains within plasmin, crucial for its function, are characterized by a central cluster of four cysteine residues involved in forming two inner disulfide bridges.

Nitrogen atoms are integral to the amino acid building blocks, while the disulfide bonds (involving sulfur atoms) play a critical role in maintaining the correct three-dimensional structure of plasmin, which is essential for its function in fibrinolysis.