The major biochemicals which People profile most commonly are proteins obtained from beef, the pancreas, plants, and through fermentation.
Let us briefly survey three particularly useful biochemical tools that could serve as the building blocks of your research.
Glutathione, a Sulfhydryl Buffer and Antioxidant:
Glutathione is a highly distinctive tripeptide formed by Glutamate, Cysteine, and Glycine residues. When present at high levels (~5mM) in cells, glutathione helps protect and repair red blood cells from oxidative stress such as from free radicals, and also detoxifies cells by reacting with peroxide, harmful waste products produced from aerobic metabolism. Glutathione can be purchased from AG Scientific, Inc in its reduced form.
The reduced thiol form of Glutathione, GSH, can become oxidized in the presence of glutathione peroxidase to form the active form GSSG, which is composed of two Glutathione tripeptide units.
A healthy ratio of GSH to GSSG in most cells is 1:500 .
Nitric Oxide, a Short-Lived Messenger Molecule:
Nitric Oxide (NO) is an important signaling molecule within many signaling-transduction processes of vertebrates. While most extracellular signals will bind to a receptor on the surface of the tartget cell, this free-radical gas is produced naturally by your cells as a short-lived mediator signal - its half life is about 5-10 seconds - for a number of physiological functions including smooth muscle contractions, blood platelets and is a prime target for scientific research.
AG Scientific has many options available including a wealth of knowledge when it comes deciding which reagent in the family of NO synthase inhibitors is best for you! Such inhibiting agents, according to the Annual Review of Pharmacology and Toxicology, are potentially beneficial in treating conditions associated with an overproduction of NO, including septic shock, neurodegenerative disorders, childhood asthma, blood flow and inflammation.
NO synthase is homologous to adenylate cyclase, but features a heme-group domain that binds NO .
Porphyrins, Important Cytoskeletal Precursors:
Porphyrin rings provide a tremendous opportunity for covalent modifcation through the chelation of metal ions. When the bare porphyrin skeleton binds to iron, an essential nutrient, it forms heme, a group of prosthetic proteins required for the synthesis of myoglobin, hemoglobin, cytochrome c, and many other proteins [Principles of Biochemistry]. Porphyrins are synthesized in both the erythroblasts and the liver, and could be the source of many disorders. The normal human erythrocyte has a life span of about 120 days, so your body keeps a store of ferric ions encased in a storage container that can hold about 4,500 ions each, for the purpose of heme synthesis.
Porphyrias are enzyme deficiency disorders within this heme biosynthetic pathway, and can either be inherited or acquired. The most prevalent of type of porphyria disorder affects the liver and is known as Acute intermittent porphyria. The disorder is characterized by overstock of porphobilinogen and delta-aminolevulinate, the precursor molecules that combine to form the square edges of the heme's porphyrin ring. The result of this overproduction is severe abdominal pain and neurological dysfunction. The "madness" of George III, King of England during the American Revolution, is reportedly to have been caused by this type of porphyria .
Amino Acids Are Precursors to Many Important Biomolecules:
In this blog we have discussed briefly how amino acids serve as precursos to a bundle of physiological biomolecules. Glutathione (gamma-Glu-Cys-Gly) works as a sulfhydryl buffer and detox agent. Nitric Oxide is a short-lived signaling molecule important for muscle movements and neurological health. Porphyrins are formed by combining glycine and succinyl CoA to produce delta-aminolevulinate which combine to form phorphobilogen. When the four molecules of phorphobilogen combine it leads to the acquisition of an iron atom which forms the heme. Cytochromes and many other functional molecules are derived from heme groups.
 Ferri, A., Fiorenzo, P., Nencini M., Cozzolino, M. Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity. 2010. Human Molecular Genetics. Oxford Journals. 19 (22): 4529-4542. doi: 10.1093/hmg/ddq383
 Hobbs, A.J., Higgs, A., and Monacada, S. Inhibition of Nitric Oxide Synthase as a Potential Therapeutic Target. 1999. Annual Review of Pharmacology and Toxicology. 39: 191-200.
 Priniciples of Biochemistry. by Jeremy M Berg, John L Tymoczko, and Lubert Stryer; W H Freedman, 5th edition, 2002. Page 659-660.