Everything below concerns NADH. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2026-06-27. Where a claim depends on a specific study, the study is described rather than over-claimed.
NAD+ is the oxidized form of nicotinamide adenine dinucleotide, a coenzyme built from two nucleotides joined by a phosphate linkage. One nucleotide carries adenine, and the other carries nicotinamide; the plus sign denotes a formal positive charge on the nicotinamide ring, not a free proton. In cells, NAD+ and its reduced partner NADH form a reversible redox pair. That pair participates in electron transfer reactions throughout metabolism. The abbreviation NAD+ is common in biochemistry, while NAD(H) sometimes denotes the combined pool.
The molecule was first described in the early twentieth century as a factor that promoted fermentation in yeast extracts. Later work linked it to hydrogen transfer and to the oxidation of nutrients in living tissues. Its structure was resolved as a dinucleotide, which explained why it could accept and donate electrons at specific enzyme sites. Today, NAD+ is recognized as a central substrate and signaling precursor, not merely a metabolic cofactor. Whether all observed NAD+ changes reflect causal signaling remains an open question.
Related compounds include NADH, the reduced form, and NADP+, which carries an additional phosphate group. NADP+ and NADPH often serve in biosynthetic and antioxidant reactions, while NAD+ and NADH are more associated with energy-yielding catabolism. Nicotinamide, nicotinic acid, and nicotinamide riboside are precursors that can enter salvage pathways. The exact contribution of dietary precursors to tissue NAD+ pools is an area of active investigation. Some studies measure labeled precursors to trace those routes.
In redox reactions, NAD+ accepts a hydride ion, which consists of two electrons and one proton. The hydride adds to the nicotinamide ring at a specific carbon, converting NAD+ into NADH. Dehydrogenase enzymes use this step in glycolysis, the citric acid cycle, and fatty acid oxidation. NADH later donates electrons to the mitochondrial electron transport chain, helping to drive ATP synthesis. The balance between NAD+ and NADH reflects the metabolic state of a cell, and shifts in that balance can alter how pathways operate.
Beyond electron transfer, NAD+ serves as a substrate for enzymes that cleave it and attach its ADP-ribose portion to other molecules. This group includes poly(ADP-ribose) polymerases, CD38, and sirtuins. Such reactions consume NAD+ and can influence its availability for metabolism. Cells replenish NAD+ through a salvage pathway that recycles nicotinamide and through routes starting from tryptophan or vitamin B3 forms. How these synthesis and consumption routes are coordinated across tissues remains an active area of study, and compartment-specific concentrations are difficult to measure directly.
Nicotinamide adenine dinucleotide, abbreviated NAD+, is a dinucleotide built from adenine, nicotinamide, two ribose sugars, and two phosphate groups. The oxidized form carries a positive charge on the nicotinamide ring, while the reduced form, NADH, is neutral. This pair acts as a reversible electron carrier in cells. NAD+ is present in bacteria, plants, animals, and fungi. Its structure allows it to accept and donate electrons without being consumed in the reactions it supports.
| Property | Value | Notes |
|---|---|---|
| Chemical name | Nicotinamide adenine dinucleotide (oxidized form) | NAD+ denotes the oxidized redox state |
| Common synonyms | Diphosphopyridine nucleotide; coenzyme I | Older names appear in historical literature |
| Molar mass | About 663.43 g/mol | Free acid value; salts and hydrates differ |
| Appearance | White to off-white powder | The purified solid is white; solutions are clear |
| Solubility | Highly soluble in water | Aqueous buffers are common laboratory solvents |
Laboratory measurement of NAD+ usually begins with rapid sample quenching because the molecule can change form after collection. Enzymatic cycling assays amplify signal through coupled reactions and are suited to small samples. High-performance liquid chromatography with ultraviolet detection separates NAD+ from related nucleotides. Liquid chromatography-mass spectrometry offers higher specificity and can distinguish NAD+ from close analogs. Each method has trade-offs in sensitivity, throughput, and equipment needs, so reported values depend heavily on extraction and detection choices.
Stability of NAD+ depends on form, temperature, pH, and water content. The solid is generally more stable than solutions, and it should be kept dry and cold. In solution, hydrolysis can cleave the dinucleotide, especially under alkaline conditions or at elevated temperature. Light exposure may also contribute to degradation. Buffers, chelating agents, and sterile handling can reduce losses, but no single condition preserves all preparations indefinitely. Researchers often prepare working solutions shortly before use and verify activity or purity after storage.
Quality control for NAD+ relies on identity, purity, and functional tests. A certificate of analysis may report high-performance liquid chromatography purity, ultraviolet spectrum, water content, and residual solvents. Because NAD+ is hygroscopic, gravimetric values can shift as material absorbs water, so purity should be interpreted alongside storage history. Mass spectrometry confirms molecular identity, while enzymatic assays show whether the material supports dehydrogenase activity. Commercial material is available as the free acid and as salts, and the counterion affects molecular weight, solubility, and how concentrations are calculated.
NAD+ is a dinucleotide composed of adenine, ribose, and nicotinamide moieties linked by phosphate groups. Its oxidized form carries a positive charge on the nicotinamide ring, which enables reversible hydride transfer. The molecule functions as a coenzyme in oxidoreductase reactions rather than as a dietary vitamin in its intact form. Cells maintain separate pools in cytoplasm, mitochondria, and nucleus. This compartmentalization allows distinct redox environments while preserving a shared chemical identity.
In glycolysis, NAD+ accepts electrons during the oxidation of glyceraldehyde-3-phosphate, forming NADH. The tricarboxylic acid cycle and fatty acid oxidation also generate NADH, which donates electrons to the mitochondrial electron transport chain. This flow supports ATP synthesis and helps maintain the redox balance of the cell. Other dehydrogenases use NAD+ as a cofactor for biosynthetic reductions and detoxification reactions. NADH is later reoxidized to sustain continued flux through these pathways.
Beyond electron transfer, NAD+ serves as a substrate for enzymes that cleave the molecule and transfer ADP-ribose units. Sirtuins, poly(ADP-ribose) polymerases, and CD38 consume NAD+ in regulatory reactions. These activities link NAD+ availability to DNA repair, chromatin modification, calcium signaling, and metabolic stress responses. Because consumption can exceed biosynthesis under some conditions, cellular NAD+ levels are dynamic rather than fixed. Enzyme affinity and local synthesis also influence how much NAD+ is available for signaling.
=== Platelet activation and platelet plug formation === When the endothelium is damaged, the normally isolated underlying collagen is exposed to circulating platelets, which bind directly to collagen with collagen-specific glycoprotein Ia/IIa surface receptors. This adhesion is strengthened further by von Willebrand factor (vWF), which is released from the endothelium and from platelets; vWF forms additional links between the platelets' glycoprotein Ib/IX/V and A1 domain. This localization of platelets to the extracellular matrix promotes collagen interaction with platelet glycoprotein VI. Binding of collagen to glycoprotein VI triggers a signaling cascade that results in activation of platelet integrins. Activated integrins mediate tight binding of platelets to the extracellular matrix. This process adheres platelets to the site of injury. Activated platelets release the contents of stored granules into the blood plasma. The granules include ADP, serotonin, platelet-activating factor (PAF), vWF, platelet factor 4, and thromboxane A2 (TXA2), which, in turn, activate additional platelets. The granules' contents activate a Gq-linked protein receptor cascade, resulting in increased calcium concentration in the platelets' cytosol. The calcium activates protein kinase C, which, in turn, activates phospholipase A2 (PLA2). PLA2 then modifies the integrin membrane glycoprotein IIb/IIIa, increasing its affinity to bind fibrinogen.
In 1981, the company was founded by two scientist/engineers from Hewlett Packard, Sam Eletr and André Marion based on technology developed by Leroy Hood and Marvin H. Caruthers. In 1982, Applied Biosystems released its first commercial instrument, the Model 470A Protein Sequencer. The machine enabled scientists to determine the order of amino acids within a purified protein, which in turn correlated with the protein's function. With 40 employees, the company, reported first-time revenue of US$402,000. In 1983, the company was led by its president and Chairman of the Board, Sam Eletr and Chief Operating Officer Andre Marion, the company doubled its number of employees to 80, and its stock went public on the NASDAQ exchange under the symbol ABIO, with revenues of US$5.9 million. A new product was a fluorescent molecular tag for immunodiagnostic assays. The company released its second commercial instrument, the Model 380A DNA Synthesizer, which made oligonucleotides, short DNA strands, for polymerase chain reaction (PCR), DNA sequencing, and gene identification. The two sequencer and synthesizer products allowed molecular biologists to clone genes by building oligonucleotides with the desired protein's DNA sequence. Automated DNA sequencing began at the California Institute of Technology, using fluorescent dyes, with Rights to the technology granted to Applied Biosystems. At CIT, Dr. Leroy Hood and Dr. Lloyd Smith, together pioneered those first DNA sequencing machines.
== Medical uses == Both corticotropin and tetracosactide have been used for diagnostic purposes to determine adrenocortical insufficiency, particularly in Addison's disease, via the ACTH stimulation test. However, as of 2015 the US label for corticotropin does not include diagnostic use. Both corticotropin and tetracosactide have been used for therapeutic purposes. In the US the tetracosactide label is limited to diagnosis but the UK label provides for therapeutic uses. In the US corticotropin is used to treat epileptic spasms in infants, acute exacerbations of multiple sclerosis in adults; acute episodes of psoriatic arthritis and rheumatoid arthritis and ankylosing spondylitis; in acute exacerbations or as maintenance therapy for collagen disorders like systemic lupus erythematosus and systemic dermatomyositis; for skin conditions like severe erythema multiforme and Stevens–Johnson syndrome; for serum sickness; for severe acute and chronic allergic and inflammatory processes involving the eye such as keratitis, iritis and iridocyclitis, diffuse posterior uveitis, choroiditis, optic neuritis, chorioretinitis, and anterior segment inflammation; sarcoidosis in the lungs; and to treat edema in certain nephrotic syndromes. In the UK tetracosactide is used for short-term therapy in conditions for which glucocorticoids are usually used but for some reason should not be; some uses include use for people who do not respond to glucocorticoids or cannot tolerate them who have ulcerative colitis, Crohn's disease, juvenile rheumatoid arthritis, rheumatoid arthritis, or osteoarthrosis.
insertion sequence (IS) Also insertion element or simply insert. Any nucleotide sequence that is inserted naturally or artificially into another sequence. The term is used in particular to refer to the part of a transposable element that codes for those proteins directly involved in the transposition process, e.g. the transposase enzyme. The coding region in a transposable insertion sequence is usually flanked by short inverted repeats, and the structure of larger transposable elements may include a pair of flanking insertion sequences which are themselves inverted.
Sources: en.wikipedia.org
until the general election after next), with the government's long-term options remaining completely open; Clarke threatened to resign if this formula were departed from. Heseltine had opposed a referendum on euro membership when Thatcher proposed it in 1990. Clarke, writing in 2016 after the Brexit Referendum, comments that he and Heseltine later agreed that they had separately decided to give way because of the pressure Major was under, and that the referendum pledge "was the biggest single mistake" of their careers, giving "legitimacy" to such a device. Heseltine made several visits to Manchester in the aftermath of the IRA bomb on 15 June 1996 – he won the praise of opposition politicians for cutting red tape to arrange remedial measures. However, Crick recounts complaints about his aloofness from small shopkeepers, and Crick comments that he seemed to have lost the common touch which he had displayed in Liverpool in the early 1980s. In 1996 Heseltine was also one of the more hawkish ministers in urging non-cooperation with the European Community over the beef ban. However, after press speculation in December 1996 that he might abandon the government's "wait and see" policy on the euro in the hope of winning Eurosceptic votes, he took to the airwaves – in apparent unison with Clarke – to insist that the government retained a free choice as to whether or not to join, angering Eurosceptics.
== External links == HPRD Human Protein Reference Database, a (manually) curated database of human protein information with visualization tools IntAct Interaction Database, a public repository for manually curated molecular interaction data from the literature DIP Database of Interacting Proteins, a manual and automatic catalog of experimentally determined interactions between proteins MIPS Mammalian Protein–Protein Interaction Database, the MIPS mammalian protein–protein interaction database
Trump consistently supported Israel, though presented himself as the "candidate of peace". Trump also supported giving weapons to Israel, likely with "no strings attached", saying that it must "finish the problem". Trump was seen by some as more pro-Israel and less sympathetic to Palestine than Biden or Harris. Trump took a hardline stance against pro-Palestinian protests, telling donors he would "crush" them and deport non-citizen protestors to "set the movement back 25 or 30 years". At times, Trump was critical of Israel's conduct, saying Israel should "get it over with ... get back to peace and stop killing people". However, he pledged to end the war in Gaza through negotiation and bring peace to the Middle East. Trump called Biden's airstrikes on Yemen "crazy" and suggested negotiating with the Houthis.
Sources: en.wikipedia.org
It indicates a formal positive charge on the nicotinamide ring. The molecule is not simply a protonated acid, and the charge is part of its redox chemistry.
NAD+ is the oxidized form, while NADH is the reduced form carrying two additional electrons and a proton. The two forms interconvert in many metabolic reactions.
No. NADP+ contains an extra phosphate group on the adenine ribose. NADP+ and NADPH tend to participate in different biosynthetic and antioxidant pathways.
It indicates the oxidized form, which has a positive charge on the nicotinamide nitrogen. The reduced partner NADH lacks that charge and carries added electrons. The plus sign is part of the standard abbreviation, not a separate ion.