Glycine

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Glycine [1]
Glycine-2D-skeletal.svg
Skeletal formula of neutral glycine
Glycine-zwitterion-2D-skeletal.svg
Skeletal formula of zwitterionic glycine
Glycine-neutral-Ipttt-conformer-3D-bs-17.png
Ball-and-stick model of the gas-phase structure
Glycine-zwitterion-from-xtal-3D-bs-17.png
Ball-and-stick model of the zwitterionic solid-state structure
Glycine-neutral-Ipttt-conformer-3D-sf.png
Space-filling model of the gas-phase structure
Glycine-zwitterion-from-xtal-3D-sf.png
Space-filling model of the zwitterionic solid-state structure
Names
IUPAC name
Glycine
Systematic IUPAC name
Aminoacetic acid [2]
Other names
  • 2-Aminoethanoic acid
  • Glycocol
  • Glycic acid
  • Dicarbamic acid
Identifiers
3D model (JSmol)
AbbreviationsGly, G
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.000.248 OOjs UI icon edit-ltr-progressive.svg
EC Number
  • 200-272-2
  • 227-841-8
E number E640 (flavour enhancer)
KEGG
PubChem CID
UNII
  • InChI=1S/C2H5NH2/c3-1-2(4)5/h1,3H2,(H,4,5) Yes check.svgY
    Key: DHMQDGOQFOQNFH-UHFFFAOYSA-N Yes check.svgY
  • InChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
    Key: DHMQDGOQFOQNFH-UHFFFAOYAW
  • C(C(=O)O)N
  • Zwitterion:C(C(=O)[O-])[NH3+]
  • C(C(=O)O)N.Cl
Properties
C2H5NO2
Molar mass 75.067 g·mol−1
AppearanceWhite solid
Density 1.1607 g/cm3 [3]
Melting point 233 °C (451 °F; 506 K) (decomposition)
249.9 g/L (25 °C) [4]
Solubility soluble in pyridine
sparingly soluble in ethanol
insoluble in ether
Acidity (pKa)2.34 (carboxyl), 9.6 (amino) [5]
-40.3·10−6 cm3/mol
Pharmacology
B05CX03 ( WHO )
Hazards
Lethal dose or concentration (LD, LC):
2600 mg/kg (mouse, oral)
Supplementary data page
Glycine (data page)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Yes check.svgY  verify  (what is  Yes check.svgYX mark.svgN ?)

Glycine (symbol Gly or G; [6] /ˈɡlaɪsiːn/ ⓘ ) [7] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable). Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8] Glycine is integral to the formation of alpha-helices in secondary protein structure due to the "flexibility" caused by such a small R group. Glycine is also an inhibitory neurotransmitter [9] – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction. [10]

It is the only achiral proteinogenic amino acid. [11] It can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom. [12]

History and etymology

Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. [13] He originally called it "sugar of gelatin", [14] [15] but French chemist Jean-Baptiste Boussingault showed in 1838 that it contained nitrogen. [16] In 1847 American scientist Eben Norton Horsford, then a student of the German chemist Justus von Liebig, proposed the name "glycocoll"; [17] [18] however, the Swedish chemist Berzelius suggested the simpler current name a year later. [19] [20] The name comes from the Greek word γλυκύς "sweet tasting" [21] (which is also related to the prefixes glyco- and gluco- , as in glycoprotein and glucose ). In 1858, the French chemist Auguste Cahours determined that glycine was an amine of acetic acid. [22]

Production

Although glycine can be isolated from hydrolyzed proteins, this route is not used for industrial production, as it can be manufactured more conveniently by chemical synthesis. [23] The two main processes are amination of chloroacetic acid with ammonia, giving glycine and hydrochloric acid, [24] and the Strecker amino acid synthesis, [25] which is the main synthetic method in the United States and Japan. [26] About 15 thousand tonnes are produced annually in this way. [27]

Glycine is also co-generated as an impurity in the synthesis of EDTA, arising from reactions of the ammonia co-product. [28]

Chemical reactions

Its acid–base properties are most important. In aqueous solution, glycine is amphoteric: below pH = 2.4, it converts to the ammonium cation called glycinium. Above about pH 9.6, it converts to glycinate.

Glycine-protonation-states-2D-skeletal.png

Glycine functions as a bidentate ligand for many metal ions, forming amino acid complexes. [29] A typical complex is Cu(glycinate)2, i.e. Cu(H2NCH2CO2)2, which exists both in cis and trans isomers. [30] [31]

With acid chlorides, glycine converts to the amidocarboxylic acid, such as hippuric acid [32] and acetylglycine. [33] With nitrous acid, one obtains glycolic acid (van Slyke determination). With methyl iodide, the amine becomes quaternized to give trimethylglycine, a natural product:

H
3N+
CH
2COO−
 + 3 CH3I → (CH
3)
3N+
CH
2COO−
 + 3 HI

Glycine condenses with itself to give peptides, beginning with the formation of glycylglycine: [34]

2 H
3N+
CH
2COO−
 → H
3N+
CH
2CONHCH
2COO−
 + H2O

Pyrolysis of glycine or glycylglycine gives 2,5-diketopiperazine, the cyclic diamide. [35]

Glycine forms esters with alcohols. They are often isolated as their hydrochloride, such as glycine methyl ester hydrochloride. Otherwise, the free ester tends to convert to diketopiperazine.

As a bifunctional molecule, glycine reacts with many reagents. These can be classified into N-centered and carboxylate-center reactions.

Metabolism

Biosynthesis

Glycine is not essential to the human diet, as it is biosynthesized in the body from the amino acid serine, which is in turn derived from 3-phosphoglycerate. In most organisms, the enzyme serine hydroxymethyltransferase catalyses this transformation via the cofactor pyridoxal phosphate: [36]

serine + tetrahydrofolate → glycine + N5,N10-methylene tetrahydrofolate + H2O

In E. coli, glycine is sensitive to antibiotics that target folate. [37]

In the liver of vertebrates, glycine synthesis is catalyzed by glycine synthase (also called glycine cleavage enzyme). This conversion is readily reversible: [36]

CO2 + NH+
4 + N5,N10-methylene tetrahydrofolate + NADH + H+ ⇌ Glycine + tetrahydrofolate + NAD +

In addition to being synthesized from serine, glycine can also be derived from threonine, choline or hydroxyproline via inter-organ metabolism of the liver and kidneys. [38]

Degradation

Glycine is degraded via three pathways. The predominant pathway in animals and plants is the reverse of the glycine synthase pathway mentioned above. In this context, the enzyme system involved is usually called the glycine cleavage system: [36]

Glycine + tetrahydrofolate + NAD+ ⇌ CO2 + NH+
4 + N5,N10-methylene tetrahydrofolate + NADH + H+

In the second pathway, glycine is degraded in two steps. The first step is the reverse of glycine biosynthesis from serine with serine hydroxymethyl transferase. Serine is then converted to pyruvate by serine dehydratase. [36]

In the third pathway of its degradation, glycine is converted to glyoxylate by D-amino acid oxidase. Glyoxylate is then oxidized by hepatic lactate dehydrogenase to oxalate in an NAD+-dependent reaction. [36]

The half-life of glycine and its elimination from the body varies significantly based on dose. [39] In one study, the half-life varied between 0.5 and 4.0 hours. [39]

Physiological function

The principal function of glycine is it acts as a precursor to proteins. Most proteins incorporate only small quantities of glycine, a notable exception being collagen, which contains about 35% glycine due to its periodically repeated role in the formation of collagen's helix structure in conjunction with hydroxyproline. [36] [40] In the genetic code, glycine is coded by all codons starting with GG, namely GGU, GGC, GGA and GGG. [8]

As a biosynthetic intermediate

In higher eukaryotes, δ-aminolevulinic acid, the key precursor to porphyrins, is biosynthesized from glycine and succinyl-CoA by the enzyme ALA synthase. Glycine provides the central C2N subunit of all purines. [36]

As a neurotransmitter

Glycine is an inhibitory neurotransmitter in the central nervous system, especially in the spinal cord, brainstem, and retina. When glycine receptors are activated, chloride enters the neuron via ionotropic receptors, causing an inhibitory postsynaptic potential (IPSP). Strychnine is a strong antagonist at ionotropic glycine receptors, whereas bicuculline is a weak one. Glycine is a required co-agonist along with glutamate for NMDA receptors. In contrast to the inhibitory role of glycine in the spinal cord, this behaviour is facilitated at the (NMDA) glutamatergic receptors which are excitatory. [41] The LD50 of glycine is 7930 mg/kg in rats (oral), [42] and it usually causes death by hyperexcitability.

As a toxin conjugation agent

Glycine conjugation pathway has not been fully investigated. [43] Glycine is thought to be a hepatic detoxifier of a number endogenous and xenobiotic organic acids. [44] Bile acids are normally conjugated to glycine in order to increase their solubility in water. [45]

The human body rapidly clears sodium benzoate by combining it with glycine to form hippuric acid which is then excreted. [46] The metabolic pathway for this begins with the conversion of benzoate by butyrate-CoA ligase into an intermediate product, benzoyl-CoA, [47] which is then metabolized by glycine N-acyltransferase into hippuric acid. [48]

Uses

In the US, glycine is typically sold in two grades: United States Pharmacopeia ("USP"), and technical grade. USP grade sales account for approximately 80 to 85 percent of the U.S. market for glycine. If purity greater than the USP standard is needed, for example for intravenous injections, a more expensive pharmaceutical grade glycine can be used. Technical grade glycine, which may or may not meet USP grade standards, is sold at a lower price for use in industrial applications, e.g., as an agent in metal complexing and finishing. [49]

Animal and human foods

Structure of cis-Cu(glycinate)2(H2O) Cu(gly)2(OH2).png
Structure of cis-Cu(glycinate)2(H2O)

Glycine is not widely used in foods for its nutritional value, except in infusions. Instead, glycine's role in food chemistry is as a flavorant. It is mildly sweet, and it counters the aftertaste of saccharine. It also has preservative properties, perhaps owing to its complexation to metal ions. Metal glycinate complexes, e.g. copper(II) glycinate are used as supplements for animal feeds. [27]

As of 1971, the U.S. Food and Drug Administration "no longer regards glycine and its salts as generally recognized as safe for use in human food", [51] and only permits food uses of glycine in certain conditions. [52]

Glycine has been researched for its potential to extend life. [53] [54] The proposed mechanisms of this effect are its ability to clear methionine from the body, and activating autophagy. [53]

Chemical feedstock

Glycine is an intermediate in the synthesis of a variety of chemical products. It is used in the manufacture of the herbicides glyphosate, [55] iprodione, glyphosine, imiprothrin, and eglinazine. [27] It is used as an intermediate of antibiotics such as thiamphenicol.[ citation needed ]

Laboratory research

Glycine is a significant component of some solutions used in the SDS-PAGE method of protein analysis. It serves as a buffering agent, maintaining pH and preventing sample damage during electrophoresis. [56] Glycine is also used to remove protein-labeling antibodies from Western blot membranes to enable the probing of numerous proteins of interest from SDS-PAGE gel. This allows more data to be drawn from the same specimen, increasing the reliability of the data, reducing the amount of sample processing, and number of samples required. [57] This process is known as stripping.

Presence in space

The presence of glycine outside the Earth was confirmed in 2009, based on the analysis of samples that had been taken in 2004 by the NASA spacecraft Stardust from comet Wild 2 and subsequently returned to Earth. Glycine had previously been identified in the Murchison meteorite in 1970. [58] The discovery of glycine in outer space bolstered the hypothesis of so-called soft-panspermia, which claims that the "building blocks" of life are widespread throughout the universe. [59] In 2016, detection of glycine within Comet 67P/Churyumov–Gerasimenko by the Rosetta spacecraft was announced. [60]

The detection of glycine outside the Solar System in the interstellar medium has been debated. [61]

Evolution

Glycine is proposed to be defined by early genetic codes. [62] [63] [64] [65] For example, low complexity regions (in proteins), that may resemble the proto-peptides of the early genetic code are highly enriched in glycine. [65]

Presence in foods

Food sources of glycine [66]
FoodPercentage
content
by weight
(g/100g)
Snacks, pork skins 11.04
Sesame seeds flour (low fat)3.43
Beverages, protein powder (soy-based)2.37
Seeds, safflower seed meal, partially defatted2.22
Meat, bison, beef and others (various parts)1.5–2.0
Gelatin desserts1.96
Seeds, pumpkin and squash seed kernels1.82
Turkey, all classes, back, meat and skin1.79
Chicken, broilers or fryers, meat and skin1.74
Pork, ground, 96% lean / 4% fat, cooked, crumbles1.71
Bacon and beef sticks1.64
Peanuts 1.63
Crustaceans, spiny lobster1.59
Spices, mustard seed, ground1.59
Salami 1.55
Nuts, butternuts, dried1.51
Fish, salmon, pink, canned, drained solids1.42
Almonds 1.42
Fish, mackerel 0.93
Cereals ready-to-eat, granola, homemade0.81
Leeks, (bulb and lower-leaf portion), freeze-dried0.7
Cheese, parmesan (and others), grated0.56
Soybeans, green, cooked, boiled, drained, without salt0.51
Bread, protein (includes gluten)0.47
Egg, whole, cooked, fried0.47
Beans, white, mature seeds, cooked, boiled, with salt0.38
Lentils, mature seeds, cooked, boiled, with salt0.37

See also

Related Research Articles

<span class="mw-page-title-main">Amino acid</span> Organic compounds containing amine and carboxylic groups

Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life.

<span class="mw-page-title-main">Phenylalanine</span> Type of α-amino acid

Phenylalanine is an essential α-amino acid with the formula C
9H
11NO
2. It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine. This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain. The L-isomer is used to biochemically form proteins coded for by DNA. Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the biological pigment melanin. It is encoded by the messenger RNA codons UUU and UUC.

<span class="mw-page-title-main">Cysteine</span> Proteinogenic amino acid

Cysteine is a semiessential proteinogenic amino acid with the formula HOOC−CH(−NH2)−CH2−SH. The thiol side chain in cysteine often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. L‑Cysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Greek κύστη kýsti, "bladder".

Serine is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC.

<span class="mw-page-title-main">Threonine</span> Amino acid

Threonine is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as E. coli. It is encoded by all the codons starting AC.

<span class="mw-page-title-main">NMDA receptor</span> Glutamate receptor and ion channel protein found in nerve cells

The N-methyl-D-aspartatereceptor (also known as the NMDA receptor or NMDAR), is a glutamate receptor and predominantly Ca2+ ion channel found in neurons. The NMDA receptor is one of three types of ionotropic glutamate receptors, the other two being AMPA and kainate receptors. Depending on its subunit composition, its ligands are glutamate and glycine (or D-serine). However, the binding of the ligands is typically not sufficient to open the channel as it may be blocked by Mg2+ ions which are only removed when the neuron is sufficiently depolarized. Thus, the channel acts as a "coincidence detector" and only once both of these conditions are met, the channel opens and it allows positively charged ions (cations) to flow through the cell membrane. The NMDA receptor is thought to be very important for controlling synaptic plasticity and mediating learning and memory functions.

<span class="mw-page-title-main">1-Aminocyclopropane-1-carboxylic acid</span> Chemical compound

1-Aminocyclopropane-1-carboxylic acid (ACC) is a disubstituted cyclic α-amino acid in which a cyclopropane ring is fused to the Cα atom of the amino acid. It is a white solid. Many cyclopropane-substituted amino acids are known, but this one occurs naturally. Like glycine, but unlike most α-amino acids, ACC is not chiral.

<span class="mw-page-title-main">Sarcosine</span> Chemical compound

Sarcosine, also known as N-methylglycine, or monomethylglycine, is a amino acid with the formula CH3N(H)CH2CO2H. It exists at neutral pH as the zwitterion CH3N+(H)2CH2CO2−, which can be obtained as a white, water-soluble powder. Like some amino acids, sarcosine converts to a cation at low pH and an anion at high pH, with the respective formulas CH3N+(H)2CH2CO2H and CH3N(H)CH2CO2−. Sarcosine is a close relative of glycine, with a secondary amine in place of the primary amine.

β-Alanine Chemical compound

β-Alanine (beta-alanine) is a naturally occurring beta amino acid, which is an amino acid in which the amino group is attached to the β-carbon instead of the more usual α-carbon for alanine (α-alanine). The IUPAC name for β-alanine is 3-aminopropanoic acid. Unlike its counterpart α-alanine, β-alanine has no stereocenter.

Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-catalyzed processes where chemical substances absorbed as nutrients serve as enzyme substrates, with conversion by the living organism either into simpler or more complex products. Examples of biosynthetic pathways include those for the production of amino acids, lipid membrane components, and nucleotides, but also for the production of all classes of biological macromolecules, and of acetyl-coenzyme A, adenosine triphosphate, nicotinamide adenine dinucleotide and other key intermediate and transactional molecules needed for metabolism. Thus, in biosynthesis, any of an array of compounds, from simple to complex, are converted into other compounds, and so it includes both the catabolism and anabolism of complex molecules. Biosynthetic processes are often represented via charts of metabolic pathways. A particular biosynthetic pathway may be located within a single cellular organelle, while others involve enzymes that are located across an array of cellular organelles and structures.

<span class="mw-page-title-main">Ligand-gated ion channel</span> Type of ion channel transmembrane protein

Ligand-gated ion channels (LICs, LGIC), also commonly referred to as ionotropic receptors, are a group of transmembrane ion-channel proteins which open to allow ions such as Na+, K+, Ca2+, and/or Cl− to pass through the membrane in response to the binding of a chemical messenger (i.e. a ligand), such as a neurotransmitter.

<span class="mw-page-title-main">Hippuric acid</span> Chemical compound

Hippuric acid is a carboxylic acid and organic compound. It is found in urine and is formed from the combination of benzoic acid and glycine. Levels of hippuric acid rise with the consumption of phenolic compounds. The phenols are first converted to benzoic acid, and then to hippuric acid and excreted in urine.

<span class="mw-page-title-main">Glycolic acid</span> Chemical compound

Glycolic acid is a colorless, odorless and hygroscopic crystalline solid, highly soluble in water. It is used in various skin-care products. Glycolic acid is widespread in nature. A glycolate is a salt or ester of glycolic acid.

<span class="mw-page-title-main">PDZ domain</span>

The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals. Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. These domains play a key role in the formation and function of signal transduction complexes. PDZ domains also play a highly significant role in the anchoring of cell surface receptors to the actin cytoskeleton via mediators like NHERF and ezrin.

<span class="mw-page-title-main">ACVR1</span> Protein-coding gene

Activin A receptor, type I (ACVR1) is a protein which in humans is encoded by the ACVR1 gene; also known as ALK-2. ACVR1 has been linked to the 2q23-24 region of the genome. This protein is important in the bone morphogenic protein (BMP) pathway which is responsible for the development and repair of the skeletal system. While knock-out models with this gene are in progress, the ACVR1 gene has been connected to fibrodysplasia ossificans progressiva, an extremely rare progressive genetic disease characterized by heterotopic ossification of muscles, tendons and ligaments. It is a bone morphogenetic protein receptor, type 1.

<span class="mw-page-title-main">D-amino acid oxidase</span> Enzyme

D-amino acid oxidase is an enzyme with the function on a molecular level to oxidize D-amino acids to the corresponding α-keto acids, producing ammonia and hydrogen peroxide. This results in a number of physiological effects in various systems, most notably the brain. The enzyme is most active toward neutral D-amino acids, and not active toward acidic D-amino acids. One of its most important targets in mammals is D-Serine in the central nervous system. By targeting this and other D-amino acids in vertebrates, DAAO is important in detoxification. The role in microorganisms is slightly different, breaking down D-amino acids to generate energy.

<span class="mw-page-title-main">Kynurenic acid</span> Chemical compound

Kynurenic acid is a product of the normal metabolism of amino acid L-tryptophan. It has been shown that kynurenic acid possesses neuroactive activity. It acts as an antiexcitotoxic and anticonvulsant, most likely through acting as an antagonist at excitatory amino acid receptors. Because of this activity, it may influence important neurophysiological and neuropathological processes. As a result, kynurenic acid has been considered for use in therapy in certain neurobiological disorders. Conversely, increased levels of kynurenic acid have also been linked to certain pathological conditions.

<span class="mw-page-title-main">Quisqualic acid</span> Chemical compound

Quisqualic acid is an agonist of the AMPA, kainate, and group I metabotropic glutamate receptors. It is one of the most potent AMPA receptor agonists known. It causes excitotoxicity and is used in neuroscience to selectively destroy neurons in the brain or spinal cord. Quisqualic acid occurs naturally in the seeds of Quisqualis species.

<span class="mw-page-title-main">Serine hydroxymethyltransferase</span> InterPro Family

Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF) to 5,10-methylenetetrahydrofolate (5,10-CH2-THF). This reaction provides the largest part of the one-carbon units available to the cell.

<span class="mw-page-title-main">Glycine cleavage system</span> Enzymes that break down glycine

The glycine cleavage system (GCS) is also known as the glycine decarboxylase complex or GDC. The system is a series of enzymes that are triggered in response to high concentrations of the amino acid glycine. The same set of enzymes is sometimes referred to as glycine synthase when it runs in the reverse direction to form glycine. The glycine cleavage system is composed of four proteins: the T-protein, P-protein, L-protein, and H-protein. They do not form a stable complex, so it is more appropriate to call it a "system" instead of a "complex". The H-protein is responsible for interacting with the three other proteins and acts as a shuttle for some of the intermediate products in glycine decarboxylation. In both animals and plants, the glycine cleavage system is loosely attached to the inner membrane of the mitochondria. Mutations in this enzymatic system are linked with glycine encephalopathy.

References

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  12. ↑ Alves A, Bassot A, Bulteau AL, Pirola L, Morio B (June 2019). "Glycine Metabolism and Its Alterations in Obesity and Metabolic Diseases". Nutrients. 11 (6): 1356. doi: 10.3390/nu11061356 . PMC   6627940 . PMID   31208147.
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  14. ↑ Braconnot H (1820). "Sur la conversion des matières animales en nouvelles substances par le moyen de l'acide sulfurique" [On the conversion of animal materials into new substances by means of sulfuric acid]. Annales de Chimie et de Physique. 2nd series (in French). 13: 113–125. ; see p. 114.
  15. ↑ MacKenzie C (1822). One Thousand Experiments in Chemistry: With Illustrations of Natural Phenomena; and Practical Observations on the Manufacturing and Chemical Processes at Present Pursued in the Successful Cultivation of the Useful Arts …. Sir R. Phillips and Company. p.  557.
  16. ↑ Boussingault (1838). "Sur la composition du sucre de gélatine et de l'acide nitro-saccharique de Braconnot" [On the composition of sugar of gelatine and of nitro-glucaric acid of Braconnot]. Comptes Rendus (in French). 7: 493–495.
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