626-72-2

Basic information

• Product Name: L-Homocystine
• Synonyms: (2S,2'S)-2,2'-Diamino-(4,4'-dithiobisbutyric acid);3,3'-(Dithiobismethylene)bisalanine;4,4'-Dithiobis[(2S)-2-aminobutanoic acid];4,4'-Dithiobis[(S)-2-aminobutanoic acid];4,4'-Dithiobis[(S)-2-aminobutyric acid];L-Homocystine ,99%;L-Homocystine,L-4,4′-Dithiobis(2-aminobutanoic acid);(2S,2'S)-4,4'-Dithiobis[2-aMinobutanoic Acid]
• CAS NO: 626-72-2
• Molecular Formula: C₈H₁₆N₂O₄S₂
• Molecular Weight: 268.35
• EINECS: 210-962-5
• Product Categories: Amines;Intermediates & Fine Chemicals;Pharmaceuticals;Sulfur & Selenium Compounds;Amino Acids
• Mol File: 626-72-2.mol
• Article Data: 10

Chemical Properties

• Melting Point: 281-284 °C (dec.)(lit.)
• Boiling Point: 507.6±50.0 °C(Predicted)
• Appearance: /
• Density: 1.443±0.06 g/cm3(Predicted)
• Storage Temp.: Store at 0-5°C
• PKA: 1.90±0.10(Predicted)
• BRN: 1728583
• CAS DataBase Reference: L-Homocystine(CAS DataBase Reference)
• NIST Chemistry Reference: L-Homocystine(626-72-2)
• EPA Substance Registry System: L-Homocystine(626-72-2)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• Hazardous Substances Data: 626-72-2(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Uses

Increased levels lead to hyperhomocysteinemia; a cardiovascular risk factor in prediction of coronary heart disease as well as being associated with congenital birth defects, pregnancy complications and cancer.

Purification Methods

The acid (3g) is dissolved in freshly boiled H2O (30mL) under N2, cooled under N2 (all operations should be under N2), absolute EtOH (100mL) is added, the acid is filtered off, and a second crop is obtained by diluting the filtrate to 500mL with absolute EtOH, kept overnight in a refrigerator, filtered, washed with EtOH and dried in a vacuum. The D(R,R)-form has similar properties but is –ve in M HCl and +ve in H2O. [du Vigneaud & Patterson J Biol Chem 109 101 1935, du Vigneaud & Brown Biochemical Preparations 5 93, 95 1975, Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 pp 2667-2670 1961, Beilstein 4 III 1643, 4 IV 3199, Koegel et al. J Am Chem Soc 77 5708 1955.]

Upstream product

• 139427-42-2 S-nitroso-L-homocysteine 
• 63-68-3 L-methionine 
• 6027-13-0 L-homocysteine 
• 75027-08-6 (S)-2-Amino-4-[(R)-2-((S)-3-amino-3-carboxy-propyldisulfanyl)-1-(carboxymethyl-carbamoyl)-ethylcarbamoyl]-butyric acid 
• 7689-60-3 S-benzyl-L-homocysteine 

Downstream Products

• 147857-42-9 L-Homocystine dimethyl ester dihydrochloride 
• 147857-42-9 methyl (2S)-2-amino-4-{[(3S)-3-amino-4-methoxy-4-oxobutyl]disulfanyl}butanoate hydrochloride 
• 144373-70-6 dimethyl 4,4'-disulfanediyl(2S,2'S)-bis(2-((tert-butoxycarbonyl)amino)butanoate) 
• 14857-77-3 L-homocysteic acid 
• 6367-73-3 S-<2-(Toluol-4-sulfonylamido)-aethyl>-L-homocystein 
• 63-68-3 L-methionine 
• 6027-13-0 L-homocysteine 
• 1601474-60-5 (2S)-2-amino-4-{[(2E)-3-phenylprop-2-en-1-yl]sulfanyl}butanoic acid 
• 1519692-32-0 (2S)-2-amino-4-{[(4-methylphenyl)methyl]sulfanyl}butanoic acid 
• 7689-60-3 S-benzyl-L-homocysteine 
• 13073-21-7 S-butyl-L-homocysteine 
• 13073-35-3 DL-ethionine 
• 13073-19-3 (2S)-2-amino-4-(propylsulfanyl)butanoic acid 
• 640272-28-2 C₁₂H₁₇NO₃S 

Relevant articles and documents

S-Adenosylhomocysteine Analogue of a Fairy Chemical, Imidazole-4-carboxamide, as its Metabolite in Rice and Yeast and Synthetic Investigations of Related Compounds

During the course of our investigations of fairy chemicals (FCs), we found S-ICAr-H (8a), as a metabolite of imidazole-4-carboxamide (ICA) in rice and yeast (Saccharomyces cerevisiae). In order to determine its absolute configuration, an efficient synthetic method of 8a was developed. This synthetic strategy was applicable to the preparation of analogues of 8a that might be biologically very important, such as S-ICAr-M (9), S-AICAr-H (10), and S-AICAr-M (11).

Crystal-facet-dependent denitrosylation: Modulation of NO release from S-nitrosothiols by Cu2O polymorphs

Nitric oxide (NO), a gaseous small molecule generated by the nitric oxide synthase (NOS) enzymes, plays key roles in signal transduction. The thiol groups present in many proteins and small molecules undergo nitrosylation to form the corresponding S-nitrosothiols. The release of NO from S-nitrosothiols is a key strategy to maintain the NO levels in biological systems. However, the controlled release of NO from the nitrosylated compounds at physiological pH remains a challenge. In this paper, we describe the synthesis and NO releasing ability of Cu2O nanomaterials and provide the first experimental evidence that the nanocrystals having different crystal facets within the same crystal system exhibit different activities toward S-nitrosothiols. We used various imaging techniques and time-dependent spectroscopic measurements to understand the nature of catalytically active species involved in the surface reactions. The denitrosylation reactions by Cu2O can be carried out multiple times without affecting the catalytic activity.

A study of the glutathione metaboloma peptides by energy-resolved mass spectrometry as a tool to investigate into the interference of toxic heavy metals with their metabolic processes

To better understand the fragmentation processes of the metal-biothiol conjugates and their possible significance in biological terms, an energy-resolved mass spectrometric study of the glutathione conjugates of heavy metals, of several thiols and disulfides of the glutathione metaboloma has been carried out. The main fragmentation process of γ-glutamyl compounds, whether in the thiol, disulfide, thioether or metal-bis-thiolate form, is the loss of the γ-glutamyl residue, a process which ERMS data showed to be hardly influenced by the sulfur substitution. However, loss of the γ-glutamyl residue from the mono-S-glutathionyl-mercury (II) cation is a much more energetic process, possibly pointing at a strong coordination of the carboxylic group to the metal. Moreover, loss of neutral mercury from ions containing the γ-glutamyl residue to yield a sulfenium cation was a much more energetic process than those not containing them, suggesting that the redox potential of the thiol/disulfide system plays a role in the formal reduction of the mercury dication in the gas phase. Occurrence of complementary sulfenium and protonated thiol fragments in the spectra of protonated disulfides of the glutathione metaboloma mirrors the thiol/disulfide redox process of biological importance. The intensity ratio of the fragments is proportional to the reduction potential in solution of the corresponding redox pairs. This finding has allowed the calculation of the previously unreported reduction potentials for the disulfide/thiol pair of cysteinylglycine, thereby confirming the decomposition scheme of bis- and mono-S-glutathionyl-mercury (II) ions. Finally, on the sole basis of the mass spectrometric fragmentation of the glutathione-mercury conjugates, and supported by independent literature evidence, an unprecedented mechanism for mercury ion-induced cellular oxidative stress could be proposed, based on the depletion of the glutathione pool by a catalytic mechanism acting on the metal (II)-thiol conjugates and involving as a necessary step the enzymatic removal of the glutamic acid residue to yield a mercury (II)-cysteinyl-glycine conjugate capable of regenerating neutral mercury through the oxidation of glutathione thiols to the corresponding disulfides. Copyright