A practical reference on mass spectrometry: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
Reviewed 2026-03-24. Anything still debated is marked as such rather than presented as settled.
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.
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.
In cells, NAD+ functions primarily as an electron carrier. Dehydrogenase enzymes in glycolysis and the citric acid cycle transfer hydride from substrates to NAD+, producing NADH. NADH then delivers electrons to the mitochondrial respiratory chain, supporting ATP synthesis. In fermentation, NADH is reoxidized to NAD+ so that glycolysis can continue. The balance between NAD+ and NADH helps set metabolic flux. Beyond redox, NAD+ serves as a substrate for enzymes that cleave it, including sirtuins, poly(ADP-ribose) polymerases, and CD38. These reactions consume NAD+ and release nicotinamide and ADP-ribose products.
Biosynthesis occurs through salvage, Preiss-Handler, and de novo pathways. In mammals, the salvage pathway from nicotinamide predominates, and NAMPT is often described as rate-limiting. Nicotinamide riboside and nicotinic acid enter related routes that converge on NAD+ production. Tissue NAD+ concentrations vary widely and are maintained by a balance of synthesis and consumption. Some studies report age-related declines in certain tissues, but whether these changes cause disease or can be reversed to improve human health remains an open question.
NAD+ stands for nicotinamide adenine dinucleotide, the oxidized form of a coenzyme found in all living cells. The molecule consists of two nucleotides, adenine and nicotinamide ribose, joined through phosphate groups. Its chemical formula is C21H27N7O14P2, and the free acid has a molar mass near 663.43 grams per mole. In redox reactions, NAD+ accepts a hydride ion and becomes NADH. The pair NAD+ and NADH participates in hundreds of metabolic reactions, including steps in glycolysis, the citric acid cycle, and oxidative phosphorylation.
| Property | Value | Notes |
|---|---|---|
| CAS number | 53-84-9 | Refers to the free acid form of NAD+. |
| Molecular formula | C21H27N7O14P2 | Free acid; salts include additional counterions. |
| UV absorbance maximum | 259-260 nm | Used for detection and concentration estimation. |
| Typical storage | -20 °C or below, desiccated | Protect from light and moisture; avoid repeated freeze-thaw. |
| Common analytical method | HPLC-UV or LC-MS | Enzymatic cycling is an alternative for low-abundance samples. |
Measuring NAD+ in biological samples requires rapid processing because the compound can degrade or interconvert after collection. Common approaches include enzymatic cycling assays, high-performance liquid chromatography, and mass spectrometry. Each method has different sensitivity, specificity, and susceptibility to interference from related nucleotides. Sample type matters: cultured cells, animal tissues, and human blood present distinct challenges. Reported values can vary widely across laboratories because of differences in extraction, normalization, and analytical platform. Standardization remains an open issue in the field.
NAD+ is relatively unstable in aqueous solution, especially at neutral or alkaline pH and at elevated temperatures. It is typically stored dry, protected from light and moisture, and kept cold or frozen for long-term use. Solutions are often prepared fresh or buffered to mildly acidic pH to slow hydrolysis. Repeated freeze-thaw cycles can reduce integrity. Laboratories may verify concentration using ultraviolet absorbance at 259 nm or by enzymatic assay. These handling practices are general laboratory conventions rather than universal rules.
Solid NAD+ is relatively stable when kept dry, cold, and protected from light. Aqueous solutions are more vulnerable to hydrolysis and can lose activity during repeated freeze-thaw cycles or prolonged storage at ambient temperature. Stability depends on pH, ionic strength, and the presence of degrading enzymes or metal ions. For many laboratory uses, aliquots are stored frozen and thawed only once. Exact degradation rates vary by matrix, so stability should be checked for each application rather than assumed.
Laboratory handling of NAD+ follows standard practices for hygroscopic fine chemicals. Personnel typically avoid inhalation and skin contact, use gloves and eye protection, and work in a ventilated area. Quality control may include ultraviolet absorbance at the nicotinamide maximum, chromatographic purity, water content, and identity confirmation by mass spectrometry. Because commercial preparations can contain counterions, residual solvents, or related nucleotides, a certificate of analysis helps verify the material. Researchers should confirm that the form supplied matches the intended assay.
Measuring NAD+ in biological samples requires care because the molecule is chemically reactive and present at low concentrations in some tissues. Common approaches include enzymatic cycling assays, high-performance liquid chromatography, and liquid chromatography coupled to mass spectrometry. Each method has different sensitivity and specificity, and sample preparation can affect results. Acidic or alkaline extraction steps are used in some protocols, but the choice depends on the analyte and matrix. No single method is universally optimal for every tissue or fluid.
NAD+ also serves as a substrate for enzymes that cleave it, including sirtuins, PARPs, and CD38. These enzymes consume NAD+ and release nicotinamide and ADP-ribose or related products. The dual roles as redox cofactor and signaling substrate connect NAD+ to DNA repair, circadian regulation, and calcium signaling. Cellular NAD+ concentrations vary by tissue, time of day, and stress exposure. How these consumption pathways interact with redox balance remains an active area of research.
NAD+ is a dinucleotide composed of two nucleotides joined by a pyrophosphate linkage. One nucleotide contains adenine, and the other contains nicotinamide. The oxidized form carries a positive charge on the nicotinamide ring and is abbreviated NAD+. It functions as a cofactor in hydride-transfer reactions, accepting electrons in catabolic pathways. In cells, it interconverts with reduced NADH, forming a redox couple central to energy metabolism. The molecule is water-soluble and does not cross cell membranes freely without specific transport or precursor pathways.
The nicotinamide ring undergoes reversible reduction at the para position, converting NAD+ to NADH. This reaction transfers a hydride equivalent, not a free hydrogen atom or electron alone. Because the redox pair has a defined reduction potential, it links oxidation of fuels to respiratory chain activity. Many dehydrogenases use NAD+ as a co-substrate and produce NADH. The ratio of NAD+ to NADH reflects metabolic state and influences flux through several pathways.
Drew insisted that there was no racial difference in human blood and that the policy would lead to needless deaths as soldiers and sailors were required to wait for "same race" blood. By the end of the war the American Red Cross had provided enough blood for over six million plasma packages. Most of the surplus plasma was returned to the United States for civilian use. Serum albumin replaced dried plasma for combat use during the Korean War.
==== December ==== On 1 December, the National Guard detained 10 people, including Sheikh Raed al-Matni, Assem Abou Fakher, Ghandi Abou Fakher, Maher Falhout, Hussam Zeidan, Zeidan Zeidan and Alameddine Zeidan, clarifying that they carried out a “swift and precise” operation to arrest what it called “traitors and conspirators”. On 3 December, Sheikh Raed al-Matni's body was found with signs of torture, after being accused of having links with the Syrian government and Suleiman Abdul Baqi. The National Guard also raided al-Baqi's house, and promised a strong response. Sheikh Maher Falhout was also killed. The National Guard was reportedly behind the killings. On 8 December, the National Guard reported mortar and drone attacks by the Syrian government forces, the affected areas are: Tel Hadid, Al-Maamel road and the Kanaker area. The National Guard declared that "the hostile fire and sources of fire were extinguished and full control of the situation on the field was restored". On 15 December, the National Guard killed the poet Anwar al-Shaer, due to their criticism of the group, in Busan, Suwayda, he was taken to the Suweida National Hospital. His brother stated that "In a cowardly and treacherous operation, the martyr of the word of truth, Anwar Fawzat Al-Shaer, the free national revolutionary poet, was murdered in front of his house" and swore revenge.
Honorary Doctorate, California State University, Fullerton (CSUF) (May 2008) NASA Performance Award (2002 & 2001) NASA Go the Extra Mile (GEM) Award (2001) NASA Superior Accomplishment Award (2000) NASA Group Achievement Award – Russian Crusader Team (2000) Camille and Henry Dreyfus Postdoctoral Fellowship in Environmental Science (1997) Outstanding Doctoral Student Award in Chemistry from the University of California, Davis (1997) American Vacuum Society – HWhetten Award (1996) American Vacuum Society Graduate Research Award (1996) Pro Femina Research Consortium Graduate Research Award (1996) Pro Femina Research Consortium Graduate Award for Scientific Travel (1996) University of California, Davis Graduate Research Award (1996) University of California, Davis Graduate Student Award for Scientific Travel (1994) Patricia Roberts Harris Graduate Fellowship in Chemistry (1993–1997) Lyle Wallace Award for Service to the Department of Chemistry, California State University Fullerton (1993) National Science Foundation Research Experience for Undergraduates Award (1992) Council of Building & Construction Trades Scholarship (1991 and 1992) Big West Scholar Athlete (1989–1991)
=== Mechanism of action === Flunarizine is a selective calcium antagonist with moderate other actions including antihistamine, serotonin receptor blocking and dopamine D2 blocking activity. Compared to other calcium channel blockers such as dihydropyridine derivatives, verapamil and diltiazem, flunarizine has low affinity to voltage-dependent calcium channels. It has been theorised that it may act not by inhibiting calcium entry into cells, but rather by an intracellular mechanism such as antagonising calmodulin, a calcium binding protein.
Sources: en.wikipedia.org
== Family == The only child of Thorburn Robertson (1851–1932), and Sarah Ann Robertson (1859-?), née Brailsford, Thorburn Brailsford Robertson was born at Edinburgh, Scotland on 4 March 1884. In the early 1890s he migrated to South Australia with his mother to join his father who was attorney for Kangarilla Silver Mines Ltd, and the manager of its copper mine at Callington, near Murray Bridge, South Australia. The Robertsons lived at Callington for a number of years.
=== Cancer === Preliminary studies suggest that FFAR2 may be involved in some types of cancer. 1) One study found that FFAR2 levels were elevated in human stomach and colorectal cancers although another study reported that FFAR2 levels were markedly deceased in human colorectal cancer. These results suggest that FFAR2 may promote the development and/or progression of human stomach cancer but its impact on human colorectal cancer requires further study. 2) In a dextran sulfate sodium-induced model of inflammation-associated colon cancer, FFAR2 knockdown mice developed larger and more tumors than control mice. This study suggests that FFAR2 inhibits the development and/or progression of inflammation-associated colon carcinoma in mice; its role in human inflammation-associated colorectal cancer (e.g., colorectal cancer developing in ulcerative colitis) has not been clarified. 3) Compared to their normal lung tissues, the lung cancer tissues of 42 patients had lower levels of FFAR2 but not FFAR1, FFAR3, or FFAR4. 4) Butyric acid inhibited the proliferation of and triggered apoptosis in cultured human A549 lung cancer cells; further studies in A549 as well as H1299 human lung cancer cells found that propionic acid inhibited their stimulated migration, invasiveness, and colony growth in cell culture assays but did not do so in FFAR2 gene knockout A549 or H1299 cells. These results suggest that FFAR2 may inhibit the development and/or progression of human lung cancer.
The outermost wall of the organ is known as the parietal layer The skin of the organ is known as the visceral layer. The organs have specialized names for their visceral fasciae. In the brain, they are known as meninges; in the heart they are known as pericardia; in the lungs, they are known as pleurae; and in the abdomen, they are known as peritonea. Visceral fascia is less extensible than superficial fascia. Due to its suspensory role for the organs, it needs to maintain its tone rather consistently. If it is too lax, it contributes to organ prolapse, yet if it is hypertonic, it restricts proper organ motility.
Sources: en.wikipedia.org
Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.
Having let slip one chance after another of reaching an accommodation with more moderate black leaders, Rhodesia's whites seem to have made the tragic choice of facing black nationalism over the barrel of a gun rather than the conference table. The downhill road toward a race war in Rhodesia is becoming increasingly slippery with blood. At this point, ZANU's alliance with FRELIMO and the porous border between Mozambique and eastern Rhodesia enabled large-scale training and infiltration of ZANU/ZANLA fighters. The governments of Zambia and Botswana were also emboldened sufficiently to allow resistance movement bases to be set up in their territories. Guerrillas began to launch operations deep inside Rhodesia, attacking roads, railways, economic targets and isolated security force positions, in 1976.
==== MeSH D12.776.422.220.286 – cytochrome c group ==== MeSH D12.776.422.220.286.100 – cytochromes c MeSH D12.776.422.220.286.150 – cytochromes c' MeSH D12.776.422.220.286.200 – cytochromes c1 MeSH D12.776.422.220.286.300 – cytochromes c2 MeSH D12.776.422.220.286.600 – cytochromes c6
From the sophistication of full fentanyl synthesis and acute toxicity in laboratory environments, 'clandestine' labs in Mexico prefer to make an illicit dosage form from available fentanyl rather than the synthesis itself. Based on further research by investigators, fentanyl and analogues are likely synthesized in labs that have the appearance of a legal entity, or are diverted from pharmaceutical laboratories. Investigations and convictions of members of the Sinaloa drug cartel by federal agencies made a clear connection between illegal arms trafficking from the U.S. to Mexico and the smuggling of fentanyl into the U.S. Mexico had repeatedly made official complaints, since illegal guns are easily purchased (for example in Arizona and as far north as Wisconsin and even Alaska) according to U.S. intelligence sources. The guns are transported onto Mexican territory through a chain of American brokers and couriers, often financed by those drug cartels that also engage in money laundering. Therefore, the lack of arms controls in the U.S. has directly contributed to the U.S. opioid overdose crisis. The opioid epidemic in the United States is largely fueled by drugs smuggled from Mexico; approximately 98% of fentanyl entering the U.S. comes from Mexico. In January 2025, President Trump said that tariffs on Mexico were intended to reduce the U.S. trade deficit and force the country to secure its border with the U.S. against fentanyl smuggling and illegal immigration.
Sources: en.wikipedia.org
Common methods include enzymatic cycling assays, HPLC with UV detection, and LC-MS. The choice depends on sample size, specificity needs, and available equipment. Rapid quenching before analysis is important because NAD+ and NADH can interconvert.
Water promotes hydrolysis, and heat accelerates degradation. Cold, dry storage slows these processes. Repeated warming and cooling can introduce moisture and condensation, so aliquoting is often used.
Yes. They may be free acid or salts, with different counterions and purity grades. The counterion changes molecular weight, so concentration calculations should account for the actual form. Certificates of analysis provide batch-specific information.
Nicotinamide adenine dinucleotide, with the plus sign indicating the oxidized form. It is a coenzyme present in all living cells. The reduced form is NADH.