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Information on EC 3.4.21.5 - thrombin and Organism(s) Bos taurus and UniProt Accession P00735
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3.4.21.5 thrombinSpecify your search results
Word Map
- 3.4.21.5
- platelet
-
anticoagulant
- heparin
- thrombosis
- bleeding
- endothelial
- artery
- thromboplastin
- collagen
- agonist
- thromboembolism
- coronary
-
procoagulant
- adp
-
antithrombotic
- venous
-
fibrinolysis
- thrombus
- hemorrhage
-
hemostatic
- hirudin
- plasminogen
-
antiplatelet
- thrombomodulin
-
protease-activated
-
arachidonic
- plasmin
-
thromboxane
-
intravascular
- viii
-
d-dimers
- atrial
- thrombocytopenia
- aspirin
- aptamer
- hypercoagulability
- willebrand
- warfarin
-
percutaneous
-
p-selectin
- rivaroxaban
-
platelet-rich
-
unfractionated
- coagulopathy
-
prothrombotic
- embolism
-
haemostasis
- diagnostics
- analysis
- hemophilia
- biotechnology
-
thrombolytic
- nutrition
- synthesis
- clopidogrel
- medicine
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
Synonyms
thrombin, alpha-thrombin, factor iia, fibrinogenase, beta-thrombin, activated factor ii, alphath, thrombin-c, thrombase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
blood-coagulation factor II, activated
-
-
-
-
blood-coagulation factor IIa
-
-
-
-
factor IIa
-
-
-
-
fibrinogenase
-
-
-
-
thrombase
-
-
-
-
thrombin, E
-
-
-
-
thrombin-C
-
-
-
-
thrombofort
-
-
-
-
topical
-
-
-
-
tropostasin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
two active site loops, residues 214-222 and residues 126-132, undergo decreases in solvent accessibility due to steric contacts with substrate. Two regions outside the active site undergo solvent protection upon substrate binding
-
CAS REGISTRY NUMBER
COMMENTARY
9002-04-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
i.e. S-2238
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
-
-
?
GLVPRGVNL + H2O
GLVPR + GVNL
-
residues 33-41 of factor XIII with mutation V34L
-
-
?
N-(4-tosyl)-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
N-(4-tosyl)-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Arg + 4-nitrophenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
-
-
-
?
protease-activated receptor + H2O
activated protease-activated receptor + ?
-
activation
-
-
?
TVELQGLVPRGVNL + H2O
TVELQGLVPR + GVNL
-
residues 28-41 of factor XIII with mutation V34L
-
-
?
factor XII + H2O
activated factor XII + ?
-
activated factor XII cross-links fibrin molecules and stabilizes the fibrin clot
-
-
?
Fibrinogen + H2O
?
-
cleavage of four Arg-Gly peptide bonds, the enzyme is involved in the final step in the coagulation of mammalian blood
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme mediates the conversion of fibrinogen to fibrin
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
activated protein C has a regulatory function in inhibiting thrombin activation, overview
-
-
?
additional information
?
-
determination of enzyme activity by active site titration with 4-nitrophenyl guanidino-benzoate
-
?
additional information
?
-
-
enzyme stimulates a marked increase in inositol phosphate accumulation, which is fully mimicked by a selective PAR1 activating peptide. Mitogenic effect of enzyme involves activation of PDGF or EGF receptors and a Gi/o-dependent activation of phosphoinositide 3-kinase. Enzyme stimulates phosphatidylinositol-3,4,5-triphosphate mass accumulation
-
-
?
additional information
?
-
-
thrombin is a multifunctional trypsin-like protease that plays a role in the blood coagulation system, stimulates platelet aggregation, and promotes its own generation through the activation of factor XI and cofactors V and VII
-
-
?
additional information
?
-
-
when binding to thrombomodulin, thrombin can activate the protein C to regulate coagulation by inhibiting thrombin generation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
factor XII + H2O
activated factor XII + ?
-
activated factor XII cross-links fibrin molecules and stabilizes the fibrin clot
-
-
?
Fibrinogen + H2O
?
-
cleavage of four Arg-Gly peptide bonds, the enzyme is involved in the final step in the coagulation of mammalian blood
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme mediates the conversion of fibrinogen to fibrin
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
activated protein C has a regulatory function in inhibiting thrombin activation, overview
-
-
?
additional information
?
-
-
enzyme stimulates a marked increase in inositol phosphate accumulation, which is fully mimicked by a selective PAR1 activating peptide. Mitogenic effect of enzyme involves activation of PDGF or EGF receptors and a Gi/o-dependent activation of phosphoinositide 3-kinase. Enzyme stimulates phosphatidylinositol-3,4,5-triphosphate mass accumulation
-
-
?
additional information
?
-
-
thrombin is a multifunctional trypsin-like protease that plays a role in the blood coagulation system, stimulates platelet aggregation, and promotes its own generation through the activation of factor XI and cofactors V and VII
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activated protein C
-
activated protein C has a regulatory function in inhibiting thrombin activation, overview
-
glycosaminoglycan AD4
-
shows only small inhibitory activity toward thrombin and the inhibition does not proceed beyond 40% inhibition
-
glycosaminoglycan AD9
-
shows only small inhibitory activity toward thrombin and the inhibition does not proceed beyond 40% inhibition
-
hemalin
-
protein of about 20 kDa, isolated from a midgut cDNA library from the hard tick Haemaphysalis longicornis. Hemalin delays bovine plasma clotting time and inhibits both thrombin-induced fibrinogen clotting and platelet aggregation. Hemalin may play a role in tick blood feeding
-
heparin
-
from porcine mucosa, inhibitory effect on fluid-phase and surface-bound thrombin in vivo in rabbits and in vitro
heparin cofactor II
-
inhibitory effect on fluid-phase and surface-bound thrombin
-
Intimatan
-
heparin cofactor II agonist, inhibitory effect on fluid-phase and surface-bound thrombin in vivo in rabbits and in vitro
isorhamnetin 3-O-(6-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside
-
slight inhibition
kaempferol 3-O-(2-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside
-
slight inhibition
thrombin inhibitor from Naja haje
-
thrombin inhibitor from Naja haje is a noncytotoxic phospholipase A2, mixed-type inhibitor of thrombin, inhibits the fibrinogenolytic and amidolytic activities of thrombin as well as its ability to induce platelet aggregation, it does not hydrolyze thrombin
-
Thrombomodulin
-
complex formation on endothelial cell surfaces blocks thrombin activity
-
additional information
-
a series of natural flavonoids as thrombin inhibitors, structure-activity relationships, molecular docking, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lung thromboplastin activator
-
the activation of bovine prothrombin occurs by bovine lung thromboplastin activator
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
thermodynamic analysis of enzyme structure
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000728
thrombin inhibitor from Naja haje
-
in 10 mM imidazole buffer (pH 7.4), at 37°C
-
additional information
additional information
inhibition kinetics for napsagatran and napsagatran ethyl ester in presence of NaCl or KCl and at 4 different temperatures
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00429
glycosaminoglycan AD4, glycosaminoglycan AD9, glycosaminoglycan AE11
Bos taurus
-
IC50 above 0.00429 mM
-
0.052
kaempferol 3-O-(2'',4''-di-(E)-p-coumaroyl)-rhamnoside
Bos taurus
-
pH and temperature not specified in the publication
0.083
kaempferol 3-O-(2''-p-coumaroyl)-rhamnoside
Bos taurus
-
pH and temperature not specified in the publication
0.0000002
thrombin inhibitor from Naja haje
Bos taurus
-
in 10 mM imidazole buffer (pH 7.4), at 37°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in human lung epithelial cells by a Rac1-dependent PI3K/Akt pathway. Treatment of cells with thrombin causes activation of Rac and Akt. Thrombin induces NF-kappaB activation and protein expression through multiple signaling pathways such as PKCalpha/c-Src, Rac1, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, IkappaB kinases, and PI3K/Akt, overview
physiological function
additional information
-
thrombin and trypsin directly activate vagal C-fibres in C57BL6 mouse lung via protease-activated receptor-1,i.e. PAR1, not via PAR3, PAR2, and PAR4, overview
physiological function
-
thrombin activation of proteinase-activated receptor 1 potentiates the myofilament Ca2+ sensitivity and induces vasoconstriction in porcine pulmonary arteries, the contractile effect of thrombin is abolished by either 4-aminidophenyl methane-sulfonyl fluoride or the proteinase-activated receptor 1 antagonist SCH79797, while it is mimicked by proteinase-activated receptor 1-activating peptide but not proteinase-activated receptor 4-activating peptide
physiological function
-
thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in human lung epithelial cells by a Rac1-dependent PI3K/Akt pathway. Treatment of cells with thrombin causes activation of Rac and Akt, the latter by Ser473 phosphorylation. Thrombin induces NF-kappaB activation and protein expression through multiple signaling pathways such as PKCalpha/c-Src, Rac1, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, IkappaB kinases, and PI3K/Akt, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). THRB_BOVIN
625
0
70506
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
-
a three-chain molecular species, 1 * 7300 + 1 * 12000 + 1 * 19500, SDS-PAGE
19500
-
a three-chain molecular species, 1 * 7300 + 1 * 12000 + 1 * 19500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complex formed with the benzamidine and Arg-based thrombin inhibitors Nalpha-(2-naphthalenesulfonyl)-glycyl-D-3-aminophenyl-alanyl-piperidine, N-alpha-tosyl-(3-amidinophenyl)alanine piperidine and (2R,4R)-4-methyl-1-[Nalpha-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulfonyl)-L-arginyl]-2-piperidine carboxylic acid
-
purified enzyme, hanging drop vapour diffusion metod, 20°C, 0.002 ml of protein in 10 mM Tris-HCl, pH 8.0, and 50 mM NaCl, is mixed with 0.002 ml of reservoir solution containing 0.1 M sodium citrate, pH 5.6, 14-16% w/v PEG 4000, and 20% w/v 2-propanol, and equilibration against 0.1 ml reservoir solution, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
immobilization of thrombin, determination of optimal conditions, overview. Application of immobilized thrombin for production of S-thanatin, small antimicrobial peptide with 21 amino acid residue, expressed in Escherichia coli strain BL21(DE3) as a fusion protein containing thrombin cleavage site. The immobilizes thrombin in polyacrylamide gel shows excellent cleavage performance within wider ranges of pH value and temperature for reaction than free enzyme, and the residual activity remain above 75% after ten times of usage
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activated protein C down-regulates thrombin formation through proteolytic inactivation of factor Va by cleavage at Arg506 and Arg306 and of factor VIIIa by cleavage at Arg336 and Arg562
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
treatment of adults with one or more mild or moderate bleeding sites not manageable by conventional modalities during elective cardiovascular, neurologic, or general surgey procedures with human or bovine thrombin, applied topically with an absorbable gelatin sponge. The proportions of patients achieving hemostasis within 10 min, 6 min or 3 min were equivalent for human and bovine thrombin.12.7% of patients who received bovine thrombin demonstrated seroconversion compared with 3.3% of the patients who received human thrombin
synthesis
-
use of thrombin as enhancer in polymerase chain reaction. Presence of bovine thrombin is exceptionally effective at preventing the formation of primer dimers and enhancing the formation of the desired polymerase chain reaction products. The PCR enhancement effects of thrombin apply to low-copy synthetic single-stranded DNAs, synthetic ssDNA pools, human genomic DNA, or hepatitis B virus genomic DNA. Thrombin is also able to effectively relieve PCR inhibition by nanomaterial inhibitors such as gold nanoparticles and graphene oxide. Compared with bovine serum albumin, thrombin is more effective and requires concentrations 18-178 times less than that of serum albumin to achieve a similar level of PCR enhancement
additional information
a modified in situ proteolysis approach is applied to specifically remove the His tag by thrombin cleavage during crystallization screening trials. This improves the morphology and diffraction quality of the crystals and allowes the acquisition of high-resolution diffraction data and structure solution
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lundblad, R.L.; Kingdon, H.S.; Mann, K.G.
Thrombin
Methods Enzymol.
45
156-176
1976
Bos taurus, Equus caballus, Homo sapiens, Sus scrofa
Lundblad, R.L.; Uhteg, L.C.; Vogel, C.N.; Kingdon, H.S.; Mann, K.G.
Preparation and partial characterization of two forms of bovine thrombin
Biochem. Biophys. Res. Commun.
66
482-489
1975
Bos taurus
Giglio, J.R.; Rossi, A.; Leone, F.A.; Chiericato, G.; Say, J.C.
Isolation and characterization of an active three-chain molecular species of bovine thrombin
Biochem. J.
159
29-33
1976
Bos taurus
Ascenzi, P.; Menegatti, E.; Bolognesi, M.; Guarneri, M.; Amiconi, G.
Catalytic properties of bovine alpha-thrombin: a comparative steady-state and pre-steady-state study
Biochim. Biophys. Acta
871
319-323
1986
Bos taurus
Brandstetter, H.; Turk, D.; Hoeffken, H.W.; Grosse, D.; Sturzebecher, J.; Martin, P.D.; Edwards, B.F.; Bode, W.
Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics
J. Mol. Biol.
226
1085-1099
1992
Bos taurus
Dullweber, F.; Stubbs, M.T.; Musil, D.; Sturzebecher, J.; Klebe, G.
Factorising ligand affinity: a combined thermodynamic and crystallographic study of trypsin and thrombin inhibition
J. Mol. Biol.
313
593-614
2001
Homo sapiens, Bos taurus (P00735)
Buchanan, M.R.; Maclean, G.A.; Brister, S.J.
Selective and sustained inhibition of surface-bound thrombin activity by intimatan/heparin cofactor II and its relevance to assessing systemic anticoagulation in vivo, ex vivo and in vitro
Thromb. Haemost.
86
909-913
2001
Bos taurus, Homo sapiens
Walker, T.R.; Cadwallader, K.A.; MacKinnon, A.; Chilvers, E.R.
Thrombin induces DNA synthesis and phosphoinositide hydrolysis in airway smooth muscle by activation of distinct receptors
Biochem. Pharmacol.
70
959-967
2005
Bos taurus
Isetti, G.; Maurer, M.C.
Thrombin activity is unaltered by N-terminal truncation of factor XIII activation peptides
Biochemistry
43
4150-4159
2004
Bos taurus
Croy, C.H.; Koeppe, J.R.; Bergqvist, S.; Komives, E.A.
Allosteric changes in solvent accessibility observed in thrombin upon active site occupation
Biochemistry
43
5246-5255
2004
Bos taurus, Homo sapiens
Iyaguchi, D.; Yao, M.; Watanabe, N.; Tanaka, I.; Toyota, E.
Crystallization and preliminary x-ray studies of the unliganded wild-type bovine thrombin
Protein Pept. Lett.
14
923-924
2007
Bos taurus
Doria, C.; Fischer, C.P.; Wood, C.G.; Li, P.M.; Marra, S.; Hart, J.
Phase 3, randomized, double-blind study of plasma-derived human thrombin versus bovine thrombin in achieving hemostasis in patients undergoing surgery
Curr. Med. Res. Opin.
24
785-794
2008
Bos taurus, Homo sapiens
Liao, M.; Zhou, J.; Gong, H.; Boldbaatar, D.; Shirafuji, R.; Battur, B.; Nishikawa, Y.; Fujisaki, K.
Hemalin, a thrombin inhibitor isolated from a midgut cDNA library from the hard tick Haemaphysalis longicornis
J. Insect Physiol.
55
164-173
2009
Bos taurus
Maki, J.; Hirano, M.; Hoka, S.; Kanaide, H.; Hirano, K.
Thrombin activation of proteinase-activated receptor 1 potentiates the myofilament Ca2+ sensitivity and induces vasoconstriction in porcine pulmonary arteries
Br. J. Pharmacol.
159
919-927
2010
Bos taurus
Zhu, H.; Hoppensteadt, D.; Adiguzel, C.; Bick, R.L.; Fareed, J.
Comparison of immunogenic potentials of bovine thrombin preparations
Clin. Appl. Thromb. Hemost.
15
41-49
2009
Bos taurus
Zhu, H.; Hoppensteadt, D.; Iqbal, O.; Litinas, E.; Adiguzel, C.; Fareed, J.
Relative purity of different bovine thrombin preparations
Clin. Appl. Thromb. Hemost.
15
681-688
2009
Bos taurus
Numakura, M.; Kusakabe, N.; Ishige, K.; Ohtake-Niimi, S.; Habuchi, H.; Habuchi, O.
Preparation of chondroitin sulfate libraries containing disulfated disaccharide units and inhibition of thrombin by these chondroitin sulfates
Glycoconj. J.
27
479-489
2010
Bos taurus
Nicolaes, G.A.; Bock, P.E.; Segers, K.; Wildhagen, K.C.; Dahlback, B.; Rosing, J.
Inhibition of thrombin formation by active site Ser360 to Ala-substituted activated protein C
J. Biol. Chem.
30
22890-22900
2010
Bos taurus
Osipov, A.V.; Filkin, S.Y.; Makarova, Y.V.; Tsetlin, V.I.; Utkin, Y.N.
A new type of thrombin inhibitor, noncytotoxic phospholipase A2, from the Naja haje cobra venom
Toxicon
55
186-194
2010
Bos taurus, Homo sapiens
Wu, G.; Deng, X.; Li, X.; Wang, X.; Wang, S.; Xu, H.
Application of immobilized thrombin for production of S-thanatin expressed in Escherichia coli
Appl. Microbiol. Biotechnol.
92
85-93
2011
Bos taurus
Lin, C.H.; Cheng, H.W.; Ma, H.P.; Wu, C.H.; Hong, C.Y.; Chen, B.C.
Thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in lung epithelial cells by a Rac1-dependent PI3K/Akt pathway
J. Biol. Chem.
286
10483-10494
2011
Bos taurus, Homo sapiens
Kwong, K.; Nassenstein, C.; de Garavilla, L.; Meeker, S.; Undem, B.J.
Thrombin and trypsin directly activate vagal C-fibres in mouse lung via protease-activated receptor-1
J. Physiol.
588
1171-1177
2010
Bos taurus
Liu, L.; Ma, H.; Yang, N.; Tang, Y.; Guo, J.; Tao, W.; Duan, J.
A series of natural flavonoids as thrombin inhibitors: structure-activity relationships
Thromb. Res.
126
e365-e378
2010
Bos taurus
Zhang, Y.; Li, X.; Zou, R.; Xue, Y.; Lou, X.; He, M.
Bovine thrombin enhances the efficiency and specificity of polymerase chain reaction
Biotechniques
57
289-294
2014
Bos taurus
Plavsa, J.J.; Rezacova, P.; Kugler, M.; Pachl, P.; Brynda, J.; Voburka, Z.; Celic, A.; Petri, E.T.; Skerlova, J.
In situ proteolysis of an N-terminal His tag with thrombin improves the diffraction quality of human aldo-keto reductase 1C3 crystals
Acta Crystallogr. Sect. F
74
300-306
2018
Bos taurus (P00735)
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