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Showing drug card for Oxytocin (DB00107)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:30
Primary Accession Number DB00107
Secondary Accession Number
  • BIOD00016
  • BTD00016
Name Oxytocin
Drug Type
  • Approved
  • Biotech
Description Synthetic 9 residue cyclic peptide. The hormone is prepared synthetically to avoid possible contamination with vasopressin (ADH) and other small polypeptides with biologic activity.
Synonyms
  1. Pitocin
  2. Syntocinon
Brand Names
  1. Oxytocin (BAM Biotech)
  2. Pitocin (Parke-Davis)
  3. Syntocinon (Sandoz)
Brand Mixtures Not Available
Chemical IUPAC Name (2S)-1-[(4R,7S,10S,13S,16S,19R)-19-amino-7-(2-amino-2-oxoethyl)-10-(3-amino-3-oxopropyl)-13-[(2S)-butan-2-yl]-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo1,2-dithia-5,8,11,14,17-pentazacycloicosane-4-carbonyl]-N-[(2S)-1-[(2-amino-2-oxoethyl)amino]-4-methyl-1-oxopentan-2-yl]pyrrolidine-2-carboxamide
Chemical Formula C43H66N12O12S2
Chemical Structure Structure
Protein Sequence(s) >DB00107 sequence 
CYIQNCPLG
CAS Registry Number 50-56-6
InChI Identifier InChI=1/C43H66N12O12S2/c1-5-22(4)35-42(66)49-26(12-13-32(45)57)38(62)51-29(17-33(46)58)39(63)53-30(20-69-68-19-25(44)36(60)50-28(40(64)54-35)16-23-8-10-24(56)11-9-23)43(67)55-14-6-7-31(55)41(65)52-27(15-21(2)3)37(61)48-18-34(47)59/h8-11,21-22,25-31,35,56H,5-7,12-20,44H2,1-4H3,(H2,45,57)(H2,46,58)(H2,47,59)(H,48,61)(H,49,66)(H,50,60)(H,51,62)(H,52,65)(H,53,63)(H,54,64)/t22-,25-,26-,27-,28-,29-,30-,31-,35-/m0/s1/f/h48-54H,45-47H2
InChI Key XNOPRXBHLZRZKH-ORQPBDEFDF
KEGG Drug D00089 Link Image
KEGG Compound C00746 Link Image
PubChem Compound 439302 Link Image
PubChem Substance 4008 Link Image
ChEBI ID Not Available
PharmGKB ID PA450760 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic3/oxytocin.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Oxytocin Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 1007.1870
Monoisotopic Molecular Weight 1006.4365
State Liquid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.49e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -2.7 Source: PhysProp
Predicted LogP -0.69 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.26 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 5.51
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1NPO Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CC[C@H](C)[C@@H]1NC(=O)[C@H](CC2=CC=C(O)C=C2)NC(=O)[C@@H](N)CSSC[C@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC1=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(=O)NCC(N)=O
Canonical SMILES CCC(C)C1NC(=O)C(CC2=CC=C(O)C=C2)NC(=O)C(N)CSSCC(NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC1=O)C(=O)N1CCCC1C(=O)NC(CC(C)C)C(=O)NCC(N)=O
Drug Category
  • Anti-tocolytic Agents
  • Labor Induction Agents
  • Oxytocics
ATC Codes
AHFS Codes
  • 76:00.00
Indication To assist in labor, elective labor induction, uterine contraction induction
Pharmacology Used to induce labor or to enhance uterine contractions during labor. Uterine motility depends on the formation of the contractile protein actomyosin under the influence of the Ca2+-dependent phosphorylating enzyme myosin light-chain kinase. Oxytocin promotes contractions by increasing the intracellular Ca2+, which in turn activates myosins light chain kinase.. Oxytocin has specific receptors in the muscle llining of the uterus and the receptor concentration increases greatly during pregnancy, reaching a maximum in early labor at term.
Mechanism of Action Binds the oxytocin receptor which leads to an increase in intracellular calcium levels.
Absorption Not Available
Toxicity Not Available
Protein Binding 30%
Biotransformation Not Available
Half Life 1-6 min
Dosage Forms
Form Route
Solution Intramuscular
Solution Intravenous
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Paquin J, Danalache BA, Jankowski M, McCann SM, Gutkowska J: Oxytocin induces differentiation of P19 embryonic stem cells to cardiomyocytes. Proc Natl Acad Sci U S A. 2002 Jul 9;99(14):9550-5. Epub 2002 Jul 1. [PubMed Link Image]
  2. Jankowski M, Danalache B, Wang D, Bhat P, Hajjar F, Marcinkiewicz M, Paquin J, McCann SM, Gutkowska J: Oxytocin in cardiac ontogeny. Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):13074-9. Epub 2004 Aug 17. [PubMed Link Image]
  3. Kosfeld M, Heinrichs M, Zak PJ, Fischbacher U, Fehr E: Oxytocin increases trust in humans. Nature. 2005 Jun 2;435(7042):673-6. [PubMed Link Image]
  4. Takayanagi Y, Yoshida M, Bielsky IF, Ross HE, Kawamata M, Onaka T, Yanagisawa T, Kimura T, Matzuk MM, Young LJ, Nishimori K: Pervasive social deficits, but normal parturition, in oxytocin receptor-deficient mice. Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):16096-101. Epub 2005 Oct 25. [PubMed Link Image]
  5. Carmichael MS, Humbert R, Dixen J, Palmisano G, Greenleaf W, Davidson JM: Plasma oxytocin increases in the human sexual response. J Clin Endocrinol Metab. 1987 Jan;64(1):27-31. [PubMed Link Image]
  6. Drugs.com Link Image
  7. Wikipedia Link Image
  8. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Oxytocin-neurophysin 1
  2. Prolyl endopeptidase
Drug Target 1 [top]
Target 1 ID 826
Target 1 Name Oxytocin-neurophysin 1
Target 1 Synonyms
  1. OT-NPI
  2. Oxytocin-neurophysin 1 precursor
Target 1 Gene Name OXT
Target 1 Protein Sequence >Oxytocin-neurophysin 1 precursor 
MAGPSLACCLLGLLALTSACYIQNCPLGGKRAAPDLDVRKCLPCGPGGKGRCFGPNICCA
EELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAVLGLCCSPDGCHADPACDAEA
TFSQR
Target 1 Number of Residues 127
Target 1 Molecular Weight 12722
Target 1 Theoretical pI 5.78
Target 1 GO Classification
Function
signal transducer activity
receptor binding
hormone activity
neuropeptide hormone activity
neurohypophyseal hormone activity
Process
Not Available
Component
extracellular region
Target 1 General Function Involved in neurohypophyseal hormone activity
Target 1 Specific Function Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-19
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 189411 Link Image
Target 1 UniProtKB/Swiss-Prot ID P01178 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name NEU1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Secreted protein
Target 1 Gene Sequence >378 bp 
ATGGCCGGCCCCAGCCTCGCTTGCTGTCTGCTCGGCCTCCTGGCGCTGACCTCCGCCTGC
TACATCCAGAACTGCCCCCTGGGAGGCAAGAGGGCCGCGCCGGACCTCGACGTGCGCAAG
TGCCTCCCCTGCGGCCCCGGGGGCAAAGGCCGCTGCTTCGGGCCCAATATCTGCTGCGCG
GAAGAGCTGGGCTGCTTCGTGGGCACCGCCGAAGCGCTGCGCTGCCAGGAGGAGAACTAC
CTGCCGTCGCCCTGCCAGTCCGGCCAGAAGGCGTGCGGGAGCGGGGGCCGCTGCGCGGTC
TTGGGCCTCTGCTGCAGCCCGGACGGCTGCCACGCCGACCCTGCCTGCGACGCGGAAGCC
ACCTTCTCCCAGCGCTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID OXT Link Image
Target 1 GenAtlas ID OXT Link Image
Target 1 HGNC ID HGNC:8528 Link Image
Target 1 Chromosome Location 20
Target 1 Locus 20p13
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Ivell R, Furuya K, Brackmann B, Dawood Y, Khan-Dawood F: Expression of the oxytocin and vasopressin genes in human and baboon gonadal tissues. Endocrinology. 1990 Dec;127(6):2990-6. [PubMed Link Image]
  3. Sausville E, Carney D, Battey J: The human vasopressin gene is linked to the oxytocin gene and is selectively expressed in a cultured lung cancer cell line. J Biol Chem. 1985 Aug 25;260(18):10236-41. [PubMed Link Image]
  4. Wood SP, Tickle IJ, Treharne AM, Pitts JE, Mascarenhas Y, Li JY, Husain J, Cooper S, Blundell TL, Hruby VJ, et al.: Crystal structure analysis of deamino-oxytocin: conformational flexibility and receptor binding. Science. 1986 May 2;232(4750):633-6. [PubMed Link Image]
  5. Rehbein M, Hillers M, Mohr E, Ivell R, Morley S, Schmale H, Richter D: The neurohypophyseal hormones vasopressin and oxytocin. Precursor structure, synthesis and regulation. Biol Chem Hoppe Seyler. 1986 Aug;367(8):695-704. [PubMed Link Image]
  6. Mohr E, Hillers M, Ivell R, Haulica ID, Richter D: Expression of the vasopressin and oxytocin genes in human hypothalami. FEBS Lett. 1985 Nov 25;193(1):12-6. [PubMed Link Image]
  7. Chauvet MT, Hurpet D, Chauvet J, Acher R: Identification of human neurophysins: complete amino acid sequences of MSEL- and VLDV-neurophysins. Proc Natl Acad Sci U S A. 1983 May;80(10):2839-43. [PubMed Link Image]
  8. Schlesinger DH, Audhya TK: A comparative study of mammalian neurophysin protein sequences. FEBS Lett. 1981 Jun 15;128(2):325-8. [PubMed Link Image]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  3. Land H, Grez M, Ruppert S, Schmale H, Rehbein M, Richter D, Schutz G: Deduced amino acid sequence from the bovine oxytocin-neurophysin I precursor cDNA. Nature. 1983 Mar 24-30;302(5906):342-4. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 3873
Target 2 Name Prolyl endopeptidase
Target 2 Synonyms
  1. EC 3.4.21.26
  2. PE
  3. Post-proline cleaving enzyme
Target 2 Gene Name PREP
Target 2 Protein Sequence >Prolyl endopeptidase 
MLSFQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRQSPNYRVINIDFWDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNI
LQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
Target 2 Number of Residues 721
Target 2 Molecular Weight 80764
Target 2 Theoretical pI 5.58
Target 2 GO Classification
Function
serine-type peptidase activity
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
serine-type endopeptidase activity
prolyl oligopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
Not Available
Target 2 General Function Amino acid transport and metabolism
Target 2 Specific Function Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long
Target 2 Pathways Not Available
Target 2 Reactions
  • Hydrolysis of ---Pro! and to a lesser extent ---Ala! in oligopeptides
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 558596 Link Image
Target 2 UniProtKB/Swiss-Prot ID P48147 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name PPCE_HUMAN Link Image
Target 2 PDB ID 1H2W Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >2133 bp 
ATGCTGTCCTTCCAGTACCCCGACGTGTACCGCGACGAGACCGCCGTACAGGATTATCAT
GGTCATAAAATTTGTGACCCTTACGCCTGGCTTGAAGACCCCGACAGTGAACAGACTAAG
GCCTTTGTGGAGGCCCAGAATAAGATTACTGTGCCATTTCTTGAGCAGTGTCCCATCAGA
GGTTTATACAAAGAGAGAATGACTGAACTATATGATTATCCCAAGTATAGTTGCCACTTC
AAGAAAGGAAAACGGTATTTTTATTTTTACAATACAGGTTTGCAGAACCAGCGAGTATTA
TATGTACAGGATTCCTTAGAGGGGGAGGCCAGAGTGTTCCTGGACCCCAACATACTGTCT
GACGATGGCACAGTGGCACTCCGAGGTTATGCGTTCAGCGAAGATGGTGAATATTTTGCC
TATGGTCTGAGTGCCAGTGGCTCAGACTGGGTGACAATCAAGTTCATGAAAGTTGATGGT
GCCAAAGAGCTTCCAGATGTGCTTGAAAGAGTCAAGTTCAGCTGTATGGCCTGGACCCAT
GATGGGAAGGGAATGTTCTACAACTCATACCCTCAACAGGATGGAAAAAGTGATGGCACA
GAGACATCTACCAATCTCCACCAAAAGCTCTACTACCATGTCTTGGGAACCGATCAGTCA
GAAGATATTTTGTGTGCTGAGTTTCCTGATGAACCTAAATGGATGGGTGGAGCTGAGTTA
TCTGATGATGGCCGCTATGTCTTGTTATCAATAAGGGAAGGATGTGATCCAGTAAACCGA
CTCTGGTACTGTGACCTACAGCAGGAATCCAGTGGCATCGCGGGAATCCTGAAGTGGGTA
AAACTGATTGACAACTTTGAAGGGGAATATGACTACGTGACCAATGAGGGGACGGTGTTC
ACATTCAAGACGAATCGCCAGTCTCCCAACTATCGCGTGATCAACATTGACTTCTGGGAT
CCTGAAGAGTCTAAGTGGAAAGTACTTGTTCCTGAGCATGAGAAAGATGTCTTAGAATGG
ATAGCTTGTGTCAGGTCCAACTTCTTGGTCTTATGCTACCTCCATGACGTCAAGAACATT
CTGCAGCTCCATGACCTGACTACTGGTGCTCTCCTTAAGACCTTCCCGCTCGATGTCGGC
AGCATTGTAGGGTACAGCGGTCAGAAGAAGGACACTGAAATCTTCTATCAGTTTACTTCC
TTTTTATCTCCAGGTATCATTTATCACTGTGATCTTACCAAAGAGGAGCTGGAGCCAAGA
GTTTTCCGAGAGGTGACCGTAAAAGGAATTGATGCTTCTGATTACCAGACAGTCCAGATT
TTCTACCCTAGCAAGGATGGTACGAAGATTCCAATGTTCATTGTGCATAAAAAAGGCATA
AAATTGGATGGCTCTCATCCAGCTTTCTTATATGGCTATGGCGGCTTCAACATATCCATC
ACACCCAACTACAGTGTTTCCAGGCTTATTTTTGTGAGACACATGGGTGGTATCCTGGCA
GTGGCCAACATCAGAGGAGGTGGCGAATATGGAGAGACGTGGCATAAAGGTGGTATCTTG
GCCAACAAACAAAACTGCTTTGATGACTTTCAGTGTGCTGCTGAGTATCTGATCAAGGAA
GGTTACACATCTCCCAAGAGGCTGACTATTAATGGAGGTTCAAATGGAGGCCTCTTAGTG
GCTGCTTGTGCAAATCAGAGACCTGACCTCTTTGGTTGTGTTATTGCCCAAGTTGGAGTA
ATGGACATGCTGAAGTTTCATAAATATACCATCGGCCATGCTTGGACCACTGATTATGGG
TGCTCGGACAGCAAACAACACTTTGAATGGCTTGTCAAATACTCTCCATTGCATAATGTG
AAGTTACCAGAAGCAGATGACATCCAGTACCCGTCCATGCTGCTCCTCACTGCTGACCAT
GATGACCGCGTGGTCCCGCTTCACTCCCTGAAGTTCATTGCCACCCTTCAGTACATCGTG
GGCCGCAGCAGGAAGCAAAGCAACCCCCTGCTTATCCACGTGGACACCAAGGCGGGCCAC
GGGGCGGGGAAGCCCACAGCCAAAGTGATAGAGGAAGTCTCAGACATGTTTGCGTTCATC
GCGCGGTGCCTGAATGTCGACTGGATTCCATAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID PREP Link Image
Target 2 GenAtlas ID PREP Link Image
Target 2 HGNC ID HGNC:9358 Link Image
Target 2 Chromosome Location 6
Target 2 Locus 6q22
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Vanhoof G, Goossens F, Hendriks L, De Meester I, Hendriks D, Vriend G, Van Broeckhoven C, Scharpe S: Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase. Gene. 1994 Nov 18;149(2):363-6. [PubMed Link Image]
  2. Shirasawa Y, Osawa T, Hirashima A: Molecular cloning and characterization of prolyl endopeptidase from human T cells. J Biochem (Tokyo). 1994 Apr;115(4):724-9. [PubMed Link Image]
Target 2 Drug References
  1. Irazusta J, Silveira PF, Gil J, Varona A, Casis L: Effects of hydrosaline treatments on prolyl endopeptidase activity in rat tissues. Regul Pept. 2001 Sep 15;101(1-3):141-7. [PubMed Link Image]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  4. Bausback HH, Ward PE: Vascular, post proline cleaving enzyme: metabolism of vasoactive peptides. Adv Exp Med Biol. 1986;198 Pt A:397-404. [PubMed Link Image]
  5. Yoshimoto T, Nishimura T, Kita T, Tsuru D: Post-proline cleaving enzyme (prolyl endopeptidase) from bovine brain. J Biochem (Tokyo). 1983 Oct;94(4):1179-90. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.