Identification
- Summary
Ferrous gluconate is a medication used to treat iron-deficiency anemia.
- Generic Name
- Ferrous gluconate
- DrugBank Accession Number
- DB14488
- Background
Not Available
- Type
- Small Molecule
- Groups
- Approved
- Structure
Structure for Ferrous gluconate (DB14488)
- Weight
- Average: 446.139
Monoisotopic: 446.035891 - Chemical Formula
- C12H22FeO14
- Synonyms
- D-gluconic acid, iron(2+) salt (2:1)
- Ferric Gluconate
- Ferrous gluconate anhydrous
- Iron(2+) gluconate (1:2)
- Iron(II) gluconate, anhydrous
Pharmacology
- Indication
Used in preventing and treating iron-deficiency anemia.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Used in combination to prevent Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• ••••••••••••• •••••••• •••••• •••••• Used in combination to treat Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• ••••••••••••• •••••••• •••••• •••••• Used in combination to treat Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• •••••••• ••••• •••••••• •••••• •••••• Used in combination to prevent Folate deficiency Combination Product in combination with: Folic acid (DB00158) •••••••••••• •••••••• ••••• •••••••• •••••• •••••• Used in combination to treat Iron deficiency Combination Product in combination with: Ascorbic acid (DB00126) •••••••••••• •••••• - Associated Therapies
- Contraindications & Blackbox Warnings
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The major activity of supplemental iron is in the prevention and treatment of iron deficiency anemia. Iron has putative immune-enhancing, anticarcinogenic and cognition-enhancing activities.
- Mechanism of action
Iron is necessary for the production of hemoglobin. Iron-deficiency can lead to decreased production of hemoglobin and a microcytic, hypochromic anemia.
Target Actions Organism UTransferrin receptor protein 1 Not Available Humans UEgl nine homolog 1 Not Available Humans UHistone deacetylase 8 Not Available Humans UAlpha-hemoglobin-stabilizing protein Not Available Humans UHemoglobin subunit alpha Not Available Humans UFrataxin, mitochondrial Not Available Humans UFerritin heavy chain Not Available Humans UFlap endonuclease 1 Not Available Humans UEndonuclease 8-like 1 Not Available Humans UEndonuclease 8-like 2 Not Available Humans UDNA polymerase beta Not Available Humans UCeruloplasmin Not Available Humans USerotransferrin Not Available Humans - Absorption
The efficiency of absorption depends on the salt form, the amount administered, the dosing regimen and the size of iron stores. Subjects with normal iron stores absorb 10% to 35% of an iron dose. Those who are iron deficient may absorb up to 95% of an iron dose.
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
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Acute iron overdosage can be divided into four stages. In the first stage, which occurs up to six hours after ingestion, the principal symptoms are vomiting and diarrhea. Other symptoms include hypotension, tachycardia and CNS depression ranging from lethargy to coma. The second phase may occur at 6-24 hours after ingestion and is characterized by a temporary remission. In the third phase, gastrointestinal symptoms recur accompanied by shock, metabolic acidosis, coma, hepatic necrosis and jaundice, hypoglycemia, renal failure and pulmonary edema. The fourth phase may occur several weeks after ingestion and is characterized by gastrointestinal obstruction and liver damage. In a young child, 75 milligrams per kilogram is considered extremely dangerous. A dose of 30 milligrams per kilogram can lead to symptoms of toxicity. Estimates of a lethal dosage range from 180 milligrams per kilogram and upwards. A peak serum iron concentration of five micrograms or more per ml is associated with moderate to severe poisoning in many.
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareAlendronic acid Ferrous gluconate can cause a decrease in the absorption of Alendronic acid resulting in a reduced serum concentration and potentially a decrease in efficacy. Almasilate Almasilate can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. Aluminium phosphate Aluminium phosphate can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. Aluminum hydroxide Aluminum hydroxide can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. Asenapine Asenapine can cause a decrease in the absorption of Ferrous gluconate resulting in a reduced serum concentration and potentially a decrease in efficacy. - Food Interactions
- Avoid milk and dairy products. Take ferrous gluconate at least 2 hours before or after milk.
- Limit caffeine intake. Food and beverages containing caffeine may reduce iron absorption.
- Take at least 2 hours before or after calcium supplements.
- Take separate from antacids. Take ferrous gluconate at least 2 hours before or after antacids.
- Take with food. This reduces gastric irritation.
- Take with foods containing vitamin C. Foods rich in vitamin C increase the absorption of iron.
Products
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Ingredient UNII CAS InChI Key Ferrous gluconate dihydrate U1B11I423Z 6047-12-7 OKGNXSFAYMSVNN-SYAJEJNSSA-L - Active Moieties
Name Kind UNII CAS InChI Key Iron unknown E1UOL152H7 7439-89-6 XEEYBQQBJWHFJM-UHFFFAOYSA-N Ferrous cation ionic GW89581OWR 15438-31-0 CWYNVVGOOAEACU-UHFFFAOYSA-N - Over the Counter Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Ferrous Gluconate Tablet 35 mg Oral Wn Pharmaceuticals Ltd. 2002-05-31 2007-08-07 Canada 
Ferrous Gluconate Tab 300mg Tablet 300 mg Oral Vita Health Products Inc 1957-12-31 2005-07-20 Canada Ferrous Gluconate Tab 300mg Tablet 300 mg / tab Oral Shoppers Drug Mart Inc. 1977-12-31 1997-08-15 Canada Ferrous Gluconate Tab 300mg Tablet 300 mg / tab Oral Pharmetics (2011) Inc. 1973-12-31 2000-08-21 Canada Ferrous Gluconate Tablet 300mg Tablet 300 mg Oral D.C. Labs Limited 1969-12-31 2005-07-19 Canada - Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Alsimine W Vitamins A D Ferrous gluconate (16 mg / amp) + Calcium glycerophosphate (13 mg / amp) + Cyanocobalamin (10 mcg / amp) + Dexpanthenol (5 mg / amp) + Dexpanthenol (400 unit / amp) + Riboflavin-5'-phosphate sodium salt dihydrate (2 mg / amp) + Nicotinamide (40 mg / amp) + Pyridoxine hydrochloride (3 mg / amp) + Thiamine hydrochloride (4.5 mg / amp) + Vitamin A (10000 unit / amp) Capsule; Liquid Oral Alsi Cie Ltee 1978-12-31 2003-05-21 Canada ANFEZINC - G SURUP Ferrous gluconate (40 mg/5mL) + Zinc gluconate (15 mg/5mL) Syrup Oral BERAT BERAN İLAÇ SAN. VE TİC. LTD. ŞTİ. 2012-08-27 2024-01-23 Turkey 
Bev 29 Tab Ferrous gluconate (1 mg / tab) + Biotin (3 mcg / tab) + Choline (63 mg / tab) + Cyanocobalamin (50 mcg / tab) + Folic acid (.013 mg / tab) + Inositol (7 mg / tab) + Niacin (1 mg / tab) + Pantothenic acid (25 mg / tab) + Riboflavin (.025 mg / tab) + Thiamine (10 mg / tab) Tablet Oral Beverly International Nutrition 1987-12-31 1998-08-01 Canada Children's Chew Multi & Min Tab Ferrous gluconate (2.5 mg / tab) + Ascorbic acid (30 mg / tab) + Beta carotene (1250 unit / tab) + Biotin (75 mcg / tab) + Calcium carbonate (100 mg / tab) + Choline bitartrate (5 mg / tab) + Copper gluconate (1 mg / tab) + Cyanocobalamin (5 mcg / tab) + DL-alpha tocopheryl acetate (15 unit / tab) + Iodine (.075 mg / tab) + Magnesium oxide (25 mg / tab) + Manganese gluconate (.5 mg / tab) + Nicotinamide (10 mg / tab) + Calcium pantothenate (6.25 mg / tab) + Potassium chloride (.5 mg / tab) + Potassium chloride (5 mg / tab) + Pyridoxine hydrochloride (1.25 mg / tab) + Riboflavin (1.25 mg / tab) + Thiamine hydrochloride (1.25 mg / tab) + Vitamin A palmitate (1250 unit / tab) + Vitamin D (200 unit / tab) + Zinc gluconate (1.25 mg / tab) Tablet Oral Natrol, Inc. 1995-12-31 2001-07-30 Canada Dynam Ampoule Et Tablet Ferrous gluconate (16 mg / 10 mL) + Ascorbic acid (150 mg / 10 mL) + Cyanocobalamin (10 mcg / 10 mL) + Dexpanthenol (5 mg / 10 mL) + Riboflavin-5'-phosphate sodium salt dihydrate (2 mg / 10 mL) + Nicotinamide (40 mg / 10 mL) + Pyridoxine hydrochloride (3 mg / 10 mL) + Thiamine hydrochloride (4.5 mg / 10 mL) + Vitamin A (5000 unit / 10 mL) + Vitamin D (400 unit / 10 mL) Liquid; Tablet Oral Cardinaux Enrg Les Produits Naturels 1989-12-31 1996-09-09 Canada - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image BioFerr 90 Ferrous gluconate dihydrate (13.2 mg/1) + Ascorbic acid (138 mg/1) + Cyanocobalamin (16.8 ug/1) + Docusate sodium (55 mg/1) + Folic acid (1.4 mg/1) + Iron (88.5 mg/1) Tablet, film coated Oral Biocomp Pharma, Inc. 2014-07-01 Not applicable US 
CitraNatal 90 DHA Ferrous gluconate dihydrate (5 mg/1) + Ascorbic acid (120 mg/1) + Calcium citrate tetrahydrate (159 mg/1) + Cupric oxide (2 mg/1) + Docusate sodium (50 mg/1) + Folic acid (1 mg/1) + Iron (85 mg/1) + Nicotinamide (20 mg/1) + Potassium Iodide (150 ug/1) + Pyridoxine hydrochloride (20 mg/1) + Riboflavin (3.4 mg/1) + Thiamine chloride (3 mg/1) + Thiamine mononitrate (4.54 mg/1) + Vitamin D (400 [iU]/1) + Zinc oxide (25 mg/1) + alpha-Tocopherol acetate (30 [iU]/1) Tablet Oral Mission Pharmacal Company 2014-04-11 Not applicable US CitraNatal Bloom Ferrous gluconate dihydrate (13.2 mg/1) + Ascorbic acid (138 mg/1) + Cyanocobalamin (16.8 ug/1) + Docusate sodium (55 mg/1) + Folic acid (1.4 mg/1) + Iron (88.5 mg/1) Tablet, film coated Oral Mission Pharmacal Company 2017-08-01 2017-07-20 US CitraNatal Bloom Ferrous gluconate dihydrate (13.2 mg/1) + Ascorbic acid (138 mg/1) + Cyanocobalamin (16.8 ug/1) + Docusate sodium (55 mg/1) + Folic acid (1.4 mg/1) + Iron (88.5 mg/1) Tablet, film coated Oral Mission Pharmacal Company 2017-08-01 2024-06-01 US CitraNatal Bloom DHA Ferrous gluconate dihydrate (1.5 mg/1) + Ascorbic acid (120 mg/1) + Crypthecodinium cohnii DHA oil (300 mg/300mg) + Cyanocobalamin (12 ug/1) + Docusate sodium (50 mg/1) + Folic acid (1 mg/1) + Iron (88.5 mg/1) Kit Oral Mission Pharmacal Company 2018-01-18 Not applicable US
Categories
- ATC Codes
- B03AD05 — Ferrous gluconate and folic acid
- B03AD — Iron in combination with folic acid
- B03A — IRON PREPARATIONS
- B03 — ANTIANEMIC PREPARATIONS
- B — BLOOD AND BLOOD FORMING ORGANS
- Drug Categories
- Classification
- Not classified
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- 781E2AXH0K
- CAS number
- 299-29-6
- InChI Key
- VRIVJOXICYMTAG-IYEMJOQQSA-L
- InChI
- InChI=1S/2C6H12O7.Fe/c2*7-1-2(8)3(9)4(10)5(11)6(12)13;/h2*2-5,7-11H,1H2,(H,12,13);/q;;+2/p-2/t2*2-,3-,4+,5-;/m11./s1
- IUPAC Name
- lambda2-iron(2+) bis((2R,3S,4R,5R)-2,3,4,5,6-pentahydroxyhexanoate)
- SMILES
- [Fe++].[H][C@@](O)(CO)[C@@]([H])(O)[C@]([H])(O)[C@@]([H])(O)C([O-])=O.[H][C@@](O)(CO)[C@@]([H])(O)[C@]([H])(O)[C@@]([H])(O)C([O-])=O
References
- General References
- TITCK Product Information: Ferrozinc-G (ferrous gluconate/zinc gluconate) oral syrup [Link]
- External Links
- PubChem Compound
- 9291
- ChemSpider
- 19953133
- Wikipedia
- Iron(II)_gluconate
Clinical Trials
- Clinical Trials
Phase Status Purpose Conditions Count 4 Completed Basic Science Anemia 1 4 Completed Diagnostic Iron Absorption / Post-gastrointestinal bypass surgery / Roux-en-Y Gastric Bypass 1 4 Completed Treatment Anemia 1 4 Completed Treatment Endometrial Cancer / Perioperative Complications / Prehabilitation 1 4 Completed Treatment Heart Failure / Iron Deficiency Anemia (IDA) 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Capsule; liquid Oral Solution Oral 6.66 mg Suspension Oral 600 mg Tablet, film coated Oral Solution Oral 3.33 g Powder, for solution Oral 126 mg Powder, for solution Oral 126 MG/10ML Powder, for solution Oral 80 MG Tablet Oral 80 MG Tablet Oral 35 mg Tablet Oral 38 mg/1 Tablet Oral 300 mg / tab Tablet Oral 300 mg Syrup Oral 35 mg / 5 mL Tablet Oral Kit Oral Capsule, liquid filled Oral Powder, for solution Oral 300 mg Tablet, effervescent Oral 650 MG Tablet Oral 35 mg / tab Powder Oral Tablet, effervescent Oral 695.04 mg Tablet Oral 695 MG Tablet, effervescent Oral Solution Oral Capsule, gelatin coated; kit; tablet Oral Syrup Oral Capsule Oral Solution, concentrate Intravenous Injection, solution, concentrate Intravenous Liquid; tablet Oral Solution Oral 650 mg Tablet, extended release Oral 35 mg / srt Tablet, extended release Oral 50 mg Liquid Oral Tablet, effervescent Oral 695 mg Tablet, sugar coated Oral Capsule - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Not Available
- Experimental Properties
- Not Available
- Predicted Properties
Property Value Source Water Solubility 36.6 mg/mL ALOGPS logP -2 ALOGPS logP -3.4 Chemaxon logS -1.1 ALOGPS pKa (Strongest Acidic) 3.39 Chemaxon pKa (Strongest Basic) -3 Chemaxon Physiological Charge -1 Chemaxon Hydrogen Acceptor Count 7 Chemaxon Hydrogen Donor Count 5 Chemaxon Polar Surface Area 141.28 Å2 Chemaxon Rotatable Bond Count 10 Chemaxon Refractivity 49.11 m3·mol-1 Chemaxon Polarizability 16.62 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
- Not Available
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Not Available
- Chromatographic Properties
Collision Cross Sections (CCS)
Not Available
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Virus receptor activity
- Specific Function
- Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferri...
- Gene Name
- TFRC
- Uniprot ID
- P02786
- Uniprot Name
- Transferrin receptor protein 1
- Molecular Weight
- 84870.665 Da
References
- Hemadi M, Ha-Duong NT, El Hage Chahine JM: The mechanism of iron release from the transferrin-receptor 1 adduct. J Mol Biol. 2006 May 12;358(4):1125-36. Epub 2006 Mar 13. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Peptidyl-proline dioxygenase activity
- Specific Function
- Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific prol...
- Gene Name
- EGLN1
- Uniprot ID
- Q9GZT9
- Uniprot Name
- Egl nine homolog 1
- Molecular Weight
- 46020.585 Da
References
- Davidson TL, Chen H, Di Toro DM, D'Angelo G, Costa M: Soluble nickel inhibits HIF-prolyl-hydroxylases creating persistent hypoxic signaling in A549 cells. Mol Carcinog. 2006 Jul;45(7):479-89. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transcription factor binding
- Specific Function
- Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an impo...
- Gene Name
- HDAC8
- Uniprot ID
- Q9BY41
- Uniprot Name
- Histone deacetylase 8
- Molecular Weight
- 41757.29 Da
References
- Gantt SL, Gattis SG, Fierke CA: Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry. 2006 May 16;45(19):6170-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia.
- Specific Function
- Hemoglobin binding
- Gene Name
- AHSP
- Uniprot ID
- Q9NZD4
- Uniprot Name
- Alpha-hemoglobin-stabilizing protein
- Molecular Weight
- 11840.325 Da
References
- Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ: Biochemical fates of alpha hemoglobin bound to alpha hemoglobin-stabilizing protein AHSP. J Biol Chem. 2006 Oct 27;281(43):32611-8. Epub 2006 Aug 10. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Oxygen transporter activity
- Specific Function
- Involved in oxygen transport from the lung to the various peripheral tissues.
- Gene Name
- HBA1
- Uniprot ID
- P69905
- Uniprot Name
- Hemoglobin subunit alpha
- Molecular Weight
- 15257.405 Da
References
- Zhou S, Olson JS, Fabian M, Weiss MJ, Gow AJ: Biochemical fates of alpha hemoglobin bound to alpha hemoglobin-stabilizing protein AHSP. J Biol Chem. 2006 Oct 27;281(43):32611-8. Epub 2006 Aug 10. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.
- Specific Function
- 2 iron, 2 sulfur cluster binding
- Gene Name
- FXN
- Uniprot ID
- Q16595
- Uniprot Name
- Frataxin, mitochondrial
- Molecular Weight
- 23134.895 Da
References
- Bencze KZ, Kondapalli KC, Cook JD, McMahon S, Millan-Pacheco C, Pastor N, Stemmler TL: The structure and function of frataxin. Crit Rev Biochem Mol Biol. 2006 Sep-Oct;41(5):269-91. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Iron ion binding
- Specific Function
- Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after ...
- Gene Name
- FTH1
- Uniprot ID
- P02794
- Uniprot Name
- Ferritin heavy chain
- Molecular Weight
- 21225.47 Da
References
- Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP: High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites. J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
- Specific Function
- 5'-3' exonuclease activity
- Gene Name
- FEN1
- Uniprot ID
- P39748
- Uniprot Name
- Flap endonuclease 1
- Molecular Weight
- 42592.635 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- Not Available
- Gene Name
- NEIL1
- Uniprot ID
- Q96FI4
- Uniprot Name
- Endonuclease 8-like 1
- Molecular Weight
- 43683.625 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Zinc ion binding
- Specific Function
- Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preferenc...
- Gene Name
- NEIL2
- Uniprot ID
- Q969S2
- Uniprot Name
- Endonuclease 8-like 2
- Molecular Weight
- 36826.285 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Microtubule binding
- Specific Function
- Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that...
- Gene Name
- POLB
- Uniprot ID
- P06746
- Uniprot Name
- DNA polymerase beta
- Molecular Weight
- 38177.34 Da
References
- Hegde ML, Hegde PM, Holthauzen LM, Hazra TK, Rao KS, Mitra S: Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J Biol Chem. 2010 Sep 10;285(37):28812-25. doi: 10.1074/jbc.M110.126664. Epub 2010 Jul 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Ferroxidase activity
- Specific Function
- Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iro...
- Gene Name
- CP
- Uniprot ID
- P00450
- Uniprot Name
- Ceruloplasmin
- Molecular Weight
- 122204.45 Da
References
- Ha-Duong NT, Eid C, Hemadi M, El Hage Chahine JM: In vitro interaction between ceruloplasmin and human serum transferrin. Biochemistry. 2010 Dec 7;49(48):10261-3. doi: 10.1021/bi1014503. Epub 2010 Nov 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transferrin receptor binding
- Specific Function
- Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from si...
- Gene Name
- TF
- Uniprot ID
- P02787
- Uniprot Name
- Serotransferrin
- Molecular Weight
- 77063.195 Da
References
- Ha-Duong NT, Eid C, Hemadi M, El Hage Chahine JM: In vitro interaction between ceruloplasmin and human serum transferrin. Biochemistry. 2010 Dec 7;49(48):10261-3. doi: 10.1021/bi1014503. Epub 2010 Nov 9. [Article]
Drug created at July 09, 2018 16:47 / Updated at April 16, 2024 12:20