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Record Information
Version2.0
Creation Date2009-03-27 00:21:36 UTC
Update Date2014-12-24 20:22:40 UTC
Accession NumberT3D0721
Identification
Common NameZinc antimonide
ClassSmall Molecule
DescriptionZinc antimonide is a chemical compound of zinc and antimony. It is used in transistors, infrared detectors and thermal imagers, as well as magnetoresistive devices. Zinc is a metallic element with the atomic number 30. It is found in nature most often as the mineral sphalerite. Though excess zinc in harmful, in smaller amounts it is an essential element for life, as it is a cofactor for over 300 enzymes and is found in just as many transcription factors. Antimony is a metallic element with the chemical symbol Sb and atomic number 51. It is a silvery white metal of medium hardness that breaks easily. Small amounts of antimony are found in the earth's crust. (11, 6, 12, 7)
Compound Type
  • Antimony Compound
  • Industrial/Workplace Toxin
  • Inorganic Compound
  • Pollutant
  • Synthetic Compound
  • Zinc Compound
Chemical Structure
Thumb
Synonyms
Synonym
Antimony, Compd. With Zinc (1:1)
Antimony, compound with zinc (1:1)
Chemical FormulaH3SbZn
Average Molecular Mass190.190 g/mol
Monoisotopic Mass187.856 g/mol
CAS Registry Number12039-35-9
IUPAC Namestibane zinc
Traditional Namestibane zinc
SMILES[Zn].[SbH3]
InChI IdentifierInChI=1S/Sb.Zn.3H
InChI KeyInChIKey=MQYGPMPHXNHXLZ-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as inorganic antimony salts. These are inorganic salts of antimony. They usually contain antimony in its ionic form.
KingdomInorganic compounds
Super ClassInorganic salts
ClassInorganic antimony salts
Sub ClassNot Available
Direct ParentInorganic antimony salts
Alternative Parents
Substituents
  • Inorganic antimony salt
  • Miscellaneous mixed metal/non-metal
  • Inorganic metalloid salt
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
StateSolid
AppearanceSilver-white crystals.
Experimental Properties
PropertyValue
Melting PointNot Available
Boiling PointNot Available
SolubilityNot Available
LogPNot Available
Predicted Properties
PropertyValueSource
logP-0.97ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity2.4 m³·mol⁻¹ChemAxon
Polarizability3.98 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
SpectraNot Available
Toxicity Profile
Route of ExposureInhalation (12) ; oral (12) ; dermal (12)
Mechanism of ToxicityAnaemia results from the excessive absorption of zinc suppressing copper and iron absorption, most likely through competitive binding of intestinal mucosal cells. Unbalanced levels of copper and zinc binding to Cu,Zn-superoxide dismutase has been linked to amyotrophic lateral sclerosis (ALS). Stomach acid dissolves metallic zinc to give corrosive zinc chloride, which can cause damage to the stomach lining. Metal fume fever is thought to be an immune response to inhaled zinc. The inhalation data suggest that the myocardium is a target of antimony toxicity. It is possible that antimony affects circulating glucose by interfering with enzymes of the glycogenolysis and gluconeogenesis pathways. The mechanism of action of antimony remains unclear. However, some studies suggest that antimony combines with sulfhydryl groups including those in several enzymes important for tissue respiration. The antidotal action of BAL depends on its ability to prevent or break the union between antimony and vital enzymes. Moreover, the The cause of death is believed to be essentially the same as that in acute arsenic poisoning. (3, 11, 2, 6, 12, 1)
MetabolismZinc can enter the body through the lungs, skin, and gastrointestinal tract. Intestinal absorption of zinc is controlled by zinc carrier protein CRIP. Zinc also binds to metallothioneins, which help prevent absorption of excess zinc. Zinc is widely distributed and found in all tissues and tissues fluids, concentrating in the liver, gastrointestinal tract, kidney, skin, lung, brain, heart, and pancreas. In the bloodstream zinc is found bound to carbonic anhydrase in erythrocytes, as well as bound to albumin, _2-macroglobulin, and amino acids in the the plasma. Albumin and amino acid bound zinc can diffuse across tissue membranes. Zinc is excreted in the urine and faeces. Antimony is widely distributed throughout the body. The hair and skin contain the highest levels of antimony. The adrenal glands, lung, large intestine, trachea, cerebellum, and kidneys also contain relatively high levels of antimony. Blood is the main vehicle for the transport of absorbed antimony to various tissue compartments of the body. Antimony is a metal and, therefore, does not undergo catabolism. Antimony can covalently interact with sulfhydryl groups and phosphate, as well as numerous reversible binding interactions with endogenous ligands (e.g., proteins). It is not known if these interactions are toxicologically significant. Antimony is excreted via the urine and feces. Some of the fecal antimony may represent unabsorbed antimony that is cleared from the lung via mucociliary action into the esophagus to the gastrointestinal tract. (11, 12)
Toxicity ValuesNot Available
Lethal DoseNot Available
Carcinogenicity (IARC Classification)No indication of carcinogenicity (not listed by IARC). (10)
Uses/SourcesZinc antimonide is used in transistors, infrared detectors and thermal imagers, as well as magnetoresistive devices. (7)
Minimum Risk LevelIntermediate Oral: 0.3 mg/kg/day (9) Chronic Oral: 0.3 mg/kg/day (9)
Health EffectsChronic exposure to zinc causes anemia, atazia, lethargy, and decreases the level of good cholesterol in the body. It is also believed to cause pancreatic and reproductive damage. Dermal exposure to antimony can cause antimony spots (papules and pustules around sweat and sebaceous glands). Antimony poisoning can also lead to pneumoconiosis. Alterations in pulmonary function and other effects including chronic bronchitis, chronic emphysema, inactive tuberculosis, pleural adhesions, and irritation can result from inhalation of antimony. Increased blood pressure can also result from antimony poisoning. Myocardial depression, vasodilation and fluid loss may cause shock with hypotension, electrolyte disturbances and acute renal failure. Cerebral oedema, coma, convulsions, and death are possible. (11, 12)
SymptomsIngestion of large doses of zinc causes stomach cramps, nausea, and vomiting. Acute inhalation of large amounts of zinc causes metal fume fever, which is characterized by chills, fever, headache, weakness, dryness of the nose and throat, chest pain, and coughing. Dermal contact with zinc results in skin irritation. Abdominal pain, vomiting, diarrhea can result from inhalation of antimony. Dyspnea, headache, vomiting,cough, conjunctivitis, and bloody purulent discharge from nose can result from inhalation exposure. Skin or eye contact can cause pain and redness of the exposed surface. (5, 11, 12)
TreatmentZinc poisoning is treated symptomatically, often by administering fluids such as water or milk, or with gastric lavage. Following oral exposure to antimony, administer charcoal as a slurry (240 mL water/30 g charcoal). Following inhalation exposure, move patient to fresh air. Monitor for respiratory distress. If cough or difficulty breathing develops, evaluate for respiratory tract irritation, bronchitis, or pneumonitis. Administer oxygen and assist ventilation as required. Treat bronchospasm with inhaled beta2 agonist and oral or parenteral corticosteroids. In case of eye exposure, irrigate exposed eyes with copious amounts of room temperature water for at least 15 minutes. Following dermal exposure, remove contaminated clothing and wash exposed area thoroughly with soap and water. A physician may need to examine the area if irritation or pain persists. (4, 12)
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDNot Available
PubChem Compound ID6336886
ChEMBL IDNot Available
ChemSpider ID4891879
KEGG IDNot Available
UniProt IDNot Available
OMIM ID
ChEBI IDNot Available
BioCyc IDNot Available
CTD IDNot Available
Stitch IDZinc antimonide
PDB IDNot Available
ACToR IDNot Available
Wikipedia LinkNot Available
References
Synthesis ReferenceNot Available
MSDSNot Available
General References
  1. Vonk WI, Klomp LW: Role of transition metals in the pathogenesis of amyotrophic lateral sclerosis. Biochem Soc Trans. 2008 Dec;36(Pt 6):1322-8. doi: 10.1042/BST0361322. [19021549 ]
  2. Poon R, Chu I, Lecavalier P, Valli VE, Foster W, Gupta S, Thomas B: Effects of antimony on rats following 90-day exposure via drinking water. Food Chem Toxicol. 1998 Jan;36(1):21-35. [9487361 ]
  3. Hayes WJ Jr. and Laws ER Jr. (eds) (1991). Handbook of Pesticide Toxicology. Volume 3. Classes of Pesticides. New York, NY: Academic Press, Inc.
  4. Rumack BH (2009). POISINDEX(R) Information System. Englewood, CO: Micromedex, Inc. CCIS Volume 141, edition expires Aug, 2009.
  5. Hamilton A and Hardy HL (1974). Industrial Toxicology. 3rd ed. Acton, MA: Publishing Sciences Group, Inc.
  6. Wikipedia. Zinc. Last Updated 24 March 2009. [Link]
  7. Wikipedia. Zinc antimonide. Last Updated 16 March 2009. [Link]
  8. Wikipedia. Metallothionein. Last Updated 20 December 2008. [Link]
  9. ATSDR - Agency for Toxic Substances and Disease Registry (2001). Minimal Risk Levels (MRLs) for Hazardous Substances. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  10. International Agency for Research on Cancer (2014). IARC Monographs on the Evaluation of Carcinogenic Risks to Humans. [Link]
  11. ATSDR - Agency for Toxic Substances and Disease Registry (1992). Toxicological profile for antimony. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  12. ATSDR - Agency for Toxic Substances and Disease Registry (2005). Toxicological profile for zinc. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available

Targets

General Function:
Glutathione transferase activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Gene Name:
GSTA1
Uniprot ID:
P08263
Molecular Weight:
25630.785 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Glutathione transferase activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Gene Name:
GSTA2
Uniprot ID:
P09210
Molecular Weight:
25663.675 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Glutathione transferase activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively.
Gene Name:
GSTA3
Uniprot ID:
Q16772
Molecular Weight:
25301.355 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Glutathione transferase activity
Specific Function:
Not Available
Gene Name:
GSTA5
Uniprot ID:
Q7RTV2
Molecular Weight:
25721.725 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Protein homodimerization activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Gene Name:
GSTM1
Uniprot ID:
P09488
Molecular Weight:
25711.555 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Receptor binding
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Gene Name:
GSTM2
Uniprot ID:
P28161
Molecular Weight:
25744.395 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Protein homodimerization activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers.
Gene Name:
GSTM3
Uniprot ID:
P21266
Molecular Weight:
26559.32 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Protein homodimerization activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Active on 1-chloro-2,4-dinitrobenzene.
Gene Name:
GSTM4
Uniprot ID:
Q03013
Molecular Weight:
25561.095 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Glutathione transferase activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Gene Name:
GSTM5
Uniprot ID:
P46439
Molecular Weight:
25674.455 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
S-nitrosoglutathione binding
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.
Gene Name:
GSTP1
Uniprot ID:
P09211
Molecular Weight:
23355.625 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Receptor binding
Specific Function:
Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
Gene Name:
GSTK1
Uniprot ID:
Q9Y2Q3
Molecular Weight:
25496.625 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Oxidoreductase activity
Specific Function:
Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.
Gene Name:
GSTO1
Uniprot ID:
P78417
Molecular Weight:
27565.6 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Oxidoreductase activity
Specific Function:
Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
Gene Name:
GSTO2
Uniprot ID:
Q9H4Y5
Molecular Weight:
28253.52 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Glutathione transferase activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide.
Gene Name:
GSTT1
Uniprot ID:
P30711
Molecular Weight:
27334.755 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Glutathione transferase activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity.
Gene Name:
GSTT2
Uniprot ID:
P0CG29
Molecular Weight:
27505.775 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Not Available
Specific Function:
Not Available
Gene Name:
Not Available
Uniprot ID:
A8MPT4
Molecular Weight:
Not Available
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Protein homodimerization activity
Specific Function:
Bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.
Gene Name:
GSTZ1
Uniprot ID:
O43708
Molecular Weight:
24212.005 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Glutathione transferase activity
Specific Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity.
Gene Name:
MGST1
Uniprot ID:
P10620
Molecular Weight:
17598.45 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Leukotriene-c4 synthase activity
Specific Function:
Can catalyze the production of LTC4 from LTA4 and reduced glutathione. Can catalyze the conjugation of 1-chloro-2,4-dinitrobenzene with reduced glutathione.
Gene Name:
MGST2
Uniprot ID:
Q99735
Molecular Weight:
16620.4 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Peroxidase activity
Specific Function:
Also functions as a glutathione peroxidase.
Gene Name:
MGST3
Uniprot ID:
O14880
Molecular Weight:
16516.185 Da
References
  1. Wikipedia. Ethanol. Last Updated 15 May 2009. [Link]
General Function:
Zinc ion binding
Specific Function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene Name:
SOD1
Uniprot ID:
P00441
Molecular Weight:
15935.685 Da
References
  1. Vonk WI, Klomp LW: Role of transition metals in the pathogenesis of amyotrophic lateral sclerosis. Biochem Soc Trans. 2008 Dec;36(Pt 6):1322-8. doi: 10.1042/BST0361322. [19021549 ]