Serotransferrin

Details

Name
Serotransferrin
Synonyms
  • Beta-1 metal-binding globulin
  • Siderophilin
  • Transferrin
Gene Name
TF
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037031|Serotransferrin
MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVK
KASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVV
KKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPC
ADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRD
QYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKE
FQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKP
VKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGK
CGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWN
IPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAF
RCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLAR
APNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKL
HDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
Number of residues
698
Molecular Weight
77063.195
Theoretical pI
7.13
GO Classification
Functions
ferric iron binding / ferric iron transmembrane transporter activity / ferrous iron binding / transferrin receptor binding
Processes
blood coagulation / cellular iron ion homeostasis / cellular response to iron ion / ferrous iron import into cell / iron ion homeostasis / platelet activation / platelet degranulation / positive regulation of receptor-mediated endocytosis / regulation of protein stability / retina homeostasis / transferrin transport / transmembrane transport
Components
apical plasma membrane / basal part of cell / basal plasma membrane / blood microparticle / cell surface / coated pit / cytoplasmic membrane-bounded vesicle / early endosome / endocytic vesicle / endosome membrane / extracellular exosome / extracellular region / extracellular space / extrinsic component of external side of plasma membrane / HFE-transferrin receptor complex / late endosome / perinuclear region of cytoplasm / recycling endosome / secretory granule lumen / vesicle
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 sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0021268|Serotransferrin (TF)
ATGAGGCTCGCCGTGGGAGCCCTGCTGGTCTGCGCCGTCCTGGGGCTGTGTCTGGCTGTC
CCTGATAAAACTGTGAGATGGTGTGCAGTGTCGGAGCATGAGGCCACTAAGTGCCAGAGT
TTCCGCGACCATATGAAAAGCGTCATTCCATCCGATGGTCCCAGTGTTGCTTGTGTGAAG
AAAGCCTCCTACCTTGATTGCATCAGGGCCATTGCGGCAAACGAAGCGGATGCTGTGACA
CTGGATGCAGGTTTGGTGTATGATGCTTACCTGGCTCCCAATAACCTGAAGCCTGTGGTG
GCAGAGTTCTATGGGTCAAAAGAGGATCCACAGACTTTCTATTATGCTGTTGCTGTGGTG
AAGAAGGATAGTGGCTTCCAGATGAACCAGCTTCGAGGCAAGAAGTCCTGCCACACGGGT
CTAGGCAGGTCCGCTGGGTGGAACATCCCCATAGGCTTACTTTACTGTGACTTACCTGAG
CCACGTAAACCTCTTGAGAAAGCAGTGGCCAATTTCTTCTCGGGCAGCTGTGCCCCTTGT
GCGGATGGGACGGACTTCCCCCAGCTGTGTCAACTGTGTCCAGGGTGTGGCTGCTCCACC
CTTAACCAATACTTCGGCTACTCGGGAGCCTTCAAGTGTCTGAAGGATGGTGCTGGGGAT
GTGGCCTTTGTCAAGCACTCGACTATATTTGAGAACTTGGCAAACAAGGCTGACAGGGAC
CAGTATGAGCTGCTTTGCCTGGACAACACCCGGAAGCCGGTAGATGAATACAAGGACTGC
CACTTGGCCCAGGTCCCTTCTCATACCGTCGTGGCCCGAAGTATGGGCGGCAAGGAGGAC
TTGATCTGGGAGCTTCTCAACCAGGCCCAGGAACATTTTGGCAAAGACAAATCAAAAGAA
TTCCAACTATTCAGCTCTCCTCATGGGAAGGACCTGCTGTTTAAGGACTCTGCCCACGGG
TTTTTAAAAGTCCCCCCCAGGATGGATGCCAAGATGTACCTGGGCTATGAGTATGTCACT
GCCATCCGGAATCTACGGGAAGGCACATGCCCAGAAGCCCCAACAGATGAATGCAAGCCT
GTGAAGTGGTGTGCGCTGAGCCACCACGAGAGGCTCAAGTGTGATGAGTGGAGTGTTAAC
AGTGTAGGGAAAATAGAGTGTGTATCAGCAGAGACCACCGAAGACTGCATCGCCAAGATC
ATGAATGGAGAAGCTGATGCCATGAGCTTGGATGGAGGGTTTGTCTACATAGCGGGCAAG
TGTGGTCTGGTGCCTGTCTTGGCAGAAAACTACAATAAGAGCGATAATTGTGAGGATACA
CCAGAGGCAGGGTATTTTGCTGTAGCAGTGGTGAAGAAATCAGCTTCTGACCTCACCTGG
GACAATCTGAAAGGCAAGAAGTCCTGCCATACGGCAGTTGGCAGAACCGCTGGCTGGAAC
ATCCCCATGGGCCTGCTCTACAATAAGATCAACCACTGCAGATTTGATGAATTTTTCAGT
GAAGGTTGTGCCCCTGGGTCTAAGAAAGACTCCAGTCTCTGTAAGCTGTGTATGGGCTCA
GGCCTAAACCTGTGTGAACCCAACAACAAAGAGGGATACTACGGCTACACAGGCGCTTTC
AGGTGTCTGGTTGAGAAGGGAGATGTGGCCTTTGTGAAACACCAGACTGTCCCACAGAAC
ACTGGGGGAAAAAACCCTGATCCATGGGCTAAGAATCTGAATGAAAAAGACTATGAGTTG
CTGTGCCTTGATGGTACCAGGAAACCTGTGGAGGAGTATGCGAACTGCCACCTGGCCAGA
GCCCCGAATCACGCTGTGGTCACACGGAAAGATAAGGAAGCTTGCGTCCACAAGATATTA
CGTCAACAGCAGCACCTATTTGGAAGCAACGTAACTGACTGCTCGGGCAACTTTTGTTTG
TTCCGGTCGGAAACCAAGGACCTTCTGTTCAGAGATGACACAGTATGTTTGGCCAAACTT
CATGACAGAAACACATATGAAAAATACTTAGGAGAAGAATATGTCAAGGCTGTTGGTAAC
CTGAGAAAATGCTCCACCTCATCACTCCTGGAAGCCTGCACTTTCCGTAGACCTTAA
Chromosome Location
3
Locus
3q22.1
External Identifiers
ResourceLink
UniProtKB IDP02787
UniProtKB Entry NameTRFE_HUMAN
GenBank Protein ID339453
GenBank Gene IDM12530
GenAtlas IDTF
HGNC IDHGNC:11740
General References
  1. Yang F, Lum JB, McGill JR, Moore CM, Naylor SL, van Bragt PH, Baldwin WD, Bowman BH: Human transferrin: cDNA characterization and chromosomal localization. Proc Natl Acad Sci U S A. 1984 May;81(9):2752-6. [PubMed:6585826]
  2. Schaeffer E, Lucero MA, Jeltsch JM, Py MC, Levin MJ, Chambon P, Cohen GN, Zakin MM: Complete structure of the human transferrin gene. Comparison with analogous chicken gene and human pseudogene. Gene. 1987;56(1):109-16. [PubMed:3678832]
  3. Hershberger CL, Larson JL, Arnold B, Rosteck PR Jr, Williams P, DeHoff B, Dunn P, O'Neal KL, Riemen MW, Tice PA, et al.: A cloned gene for human transferrin. Ann N Y Acad Sci. 1991 Dec 27;646:140-54. [PubMed:1809186]
  4. Beutler E, Gelbart T, Lee P, Trevino R, Fernandez MA, Fairbanks VF: Molecular characterization of a case of atransferrinemia. Blood. 2000 Dec 15;96(13):4071-4. [PubMed:11110675]
  5. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed:16641997]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  7. Adrian GS, Korinek BW, Bowman BH, Yang F: The human transferrin gene: 5' region contains conserved sequences which match the control elements regulated by heavy metals, glucocorticoids and acute phase reaction. Gene. 1986;49(2):167-75. [PubMed:3106157]
  8. Lucero MA, Schaeffer E, Cohen GN, Zakin MM: The 5' region of the human transferrin gene: structure and potential regulatory sites. Nucleic Acids Res. 1986 Nov 11;14(21):8692. [PubMed:3786138]
  9. MacGillivray RT, Mendez E, Shewale JG, Sinha SK, Lineback-Zins J, Brew K: The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. J Biol Chem. 1983 Mar 25;258(6):3543-53. [PubMed:6833213]
  10. de Arriba Zerpa GA, Saleh MC, Fernandez PM, Guillou F, Espinosa de los Monteros A, de Vellis J, Zakin MM, Baron B: Alternative splicing prevents transferrin secretion during differentiation of a human oligodendrocyte cell line. J Neurosci Res. 2000 Aug 15;61(4):388-95. [PubMed:10931525]
  11. Park I, Schaeffer E, Sidoli A, Baralle FE, Cohen GN, Zakin MM: Organization of the human transferrin gene: direct evidence that it originated by gene duplication. Proc Natl Acad Sci U S A. 1985 May;82(10):3149-53. [PubMed:3858812]
  12. Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9. [PubMed:7498159]
  13. Uzan G, Frain M, Park I, Besmond C, Maessen G, Trepat JS, Zakin MM, Kahn A: Molecular cloning and sequence analysis of cDNA for human transferrin. Biochem Biophys Res Commun. 1984 Feb 29;119(1):273-81. [PubMed:6322780]
  14. Namekata K, Oyama F, Imagawa M, Ihara Y: Human transferrin (Tf): a single mutation at codon 570 determines Tf C1 or Tf C2 variant. Hum Genet. 1997 Sep;100(3-4):457-8. [PubMed:9272172]
  15. Duguid JR, Bohmont CW, Liu NG, Tourtellotte WW: Changes in brain gene expression shared by scrapie and Alzheimer disease. Proc Natl Acad Sci U S A. 1989 Sep;86(18):7260-4. [PubMed:2780570]
  16. MacGillivray RT, Mendez E, Sinha SK, Sutton MR, Lineback-Zins J, Brew K: The complete amino acid sequence of human serum transferrin. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2504-8. [PubMed:6953407]
  17. Woodworth RC, Mason AB, Funk WD, MacGillivray RT: Expression and initial characterization of five site-directed mutants of the N-terminal half-molecule of human transferrin. Biochemistry. 1991 Nov 12;30(45):10824-9. [PubMed:1932003]
  18. Kristiansen TZ, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P, Goggins MG, Maitra A, Pandey A: A proteomic analysis of human bile. Mol Cell Proteomics. 2004 Jul;3(7):715-28. Epub 2004 Apr 14. [PubMed:15084671]
  19. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed:14760718]
  20. Satomi Y, Shimonishi Y, Hase T, Takao T: Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry. Rapid Commun Mass Spectrom. 2004;18(24):2983-8. [PubMed:15536627]
  21. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952]
  22. Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed:16740002]
  23. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218]
  24. Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [PubMed:19139490]
  25. Nilsson J, Ruetschi U, Halim A, Hesse C, Carlsohn E, Brinkmalm G, Larson G: Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009 Nov;6(11):809-11. doi: 10.1038/nmeth.1392. Epub 2009 Oct 18. [PubMed:19838169]
  26. Rosenow A, Noben JP, Jocken J, Kallendrusch S, Fischer-Posovszky P, Mariman EC, Renes J: Resveratrol-induced changes of the human adipocyte secretion profile. J Proteome Res. 2012 Sep 7;11(9):4733-43. doi: 10.1021/pr300539b. Epub 2012 Aug 27. [PubMed:22905912]
  27. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  28. Tagliabracci VS, Wiley SE, Guo X, Kinch LN, Durrant E, Wen J, Xiao J, Cui J, Nguyen KB, Engel JL, Coon JJ, Grishin N, Pinna LA, Pagliarini DJ, Dixon JE: A Single Kinase Generates the Majority of the Secreted Phosphoproteome. Cell. 2015 Jun 18;161(7):1619-32. doi: 10.1016/j.cell.2015.05.028. [PubMed:26091039]
  29. MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN: Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. Biochemistry. 1998 Jun 2;37(22):7919-28. [PubMed:9609685]
  30. Jeffrey PD, Bewley MC, MacGillivray RT, Mason AB, Woodworth RC, Baker EN: Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin. Biochemistry. 1998 Oct 6;37(40):13978-86. [PubMed:9760232]
  31. Bewley MC, Tam BM, Grewal J, He S, Shewry S, Murphy ME, Mason AB, Woodworth RC, Baker EN, MacGillivray RT: X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32. Biochemistry. 1999 Feb 23;38(8):2535-41. [PubMed:10029548]
  32. Evans P, Kemp J: Exon/intron structure of the human transferrin receptor gene. Gene. 1997 Oct 15;199(1-2):123-31. [PubMed:9358047]
  33. Pang H, Koda Y, Soejima M, Kimura H: Identification of a mutation (A1879G) of transferrin from cDNA prepared from peripheral blood cells. Ann Hum Genet. 1998 May;62(Pt 3):271-4. [PubMed:9803271]
  34. Lee PL, Halloran C, Trevino R, Felitti V, Beutler E: Human transferrin G277S mutation: a risk factor for iron deficiency anaemia. Br J Haematol. 2001 Nov;115(2):329-33. [PubMed:11703331]
  35. Douabin-Gicquel V, Soriano N, Ferran H, Wojcik F, Palierne E, Tamim S, Jovelin T, McKie AT, Le Gall JY, David V, Mosser J: Identification of 96 single nucleotide polymorphisms in eight genes involved in iron metabolism: efficiency of bioinformatic extraction compared with a systematic sequencing approach. Hum Genet. 2001 Oct;109(4):393-401. [PubMed:11702220]
  36. Knisely AS, Gelbart T, Beutler E: Molecular characterization of a third case of human atransferrinemia. Blood. 2004 Oct 15;104(8):2607. [PubMed:15466165]
  37. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01370Aluminiumapproved, investigationalunknownDetails
DB00893Iron Dextranapproved, vet_approvedunknownsubstrateDetails
DB01294Bismuth subsalicylateapproved, vet_approvedunknownDetails
DB05260Gallium nitrateapproved, investigationalunknownsubstrateDetails
DB09146Iron sucroseapprovedunknownsubstratecarrierDetails
DB09130Copperapproved, investigationalunknownDetails
DB00515CisplatinapprovedunknownDetails
DB11397Dichlorvosvet_approvedunknownDetails
DB00677Isoflurophateapproved, investigational, withdrawnunknownDetails
DB01592IronapprovedunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB06757Manganeseapproved, nutraceuticalunknownDetails
DB11136ChromiumapprovedunknownbinderDetails
DB11182Rose bengalapproved, investigationalunknownbinderDetails
DB06215Ferumoxytolapproved, investigationalyestransporterDetails
DB13257Ferrous sulfate anhydrousapprovedyestransporterDetails
DB13949Ferric cationapprovedunknownbinderDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14488Ferrous gluconateapprovedunknownDetails
DB14489Ferrous succinateapprovedunknownDetails
DB14490Ferrous ascorbateapprovedunknownDetails
DB14491Ferrous fumarateapprovedunknownDetails
DB14501Ferrous glycine sulfateapprovedunknownDetails
DB14517Aluminium phosphateapproved, investigationalunknownDetails
DB14518Aluminum acetateapproved, investigationalunknownDetails
DB14520Tetraferric tricitrate decahydrateapprovedunknownDetails
DB14526Chromic citrateexperimentalunknownDetails
DB14527Chromic nitrateapprovedunknownDetails
DB14528Chromium gluconateapprovedunknownDetails
DB14529Chromium nicotinateapproved, experimentalunknownDetails
DB14530Chromous sulfateapprovedunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails