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Information on EC 3.4.21.4 - trypsin and Organism(s) Sus scrofa and UniProt Accession P00761
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3.4.21.4 trypsinSpecify your search results
Word Map
- 3.4.21.4
- soybean
- pancreas
- elastase
- pepsin
- thrombin
- amylase
- proteinases
- albumin
- lipase
- porcine
- collagenase
- pronase
- erythrocyte
- plasmin
- collagen
- kallikreins
- sephadex
- neuraminidase
- bean
- lectin
-
exocrine
- carboxypeptidase
- juice
- cathepsins
- coagulation
-
edman
- casein
- duodenal
- plasminogen
-
acinar
- aprotinin
-
cyanogen
- subtilisin
- zymogen
- heparin
-
radioimmunoassay
- midguts
- cholecystokinin
-
reversed-phase
- lysozyme
- venom
-
125i-labeled
- hydrolysates
-
protease-activated
- kinin
- tryptase
- flour
- phosphopeptides
-
hemagglutination
- hyaluronidase
- biotechnology
- synthesis
- food industry
- medicine
- analysis
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
trypsin, at-ii, cationic trypsinogen, beta-trypsin, trypsin-like enzyme, mesotrypsin, trypsin a, cationic trypsin, anionic trypsinogen, anionic trypsin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-trypsin
-
-
-
-
Anionic trypsinogen
-
-
-
-
beta-trypsin
-
-
-
-
Brain trypsinogen
-
-
-
-
Cationic trypsinogen
-
-
-
-
cocoonase
-
-
-
-
Mesotrypsinogen
-
-
-
-
parenzyme
-
-
-
-
parenzymol
-
-
-
-
pseudotrypsin
-
-
-
-
SET
-
-
-
-
sperm receptor hydrolase
-
-
-
-
tripcellim
-
-
-
-
tryptar
-
-
-
-
tryptase
-
-
-
-
trypure
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY
9002-07-7
-
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
(benzyloxycarbonyl-L-alanyl-L-arginine)2-rhodamine-110 + 2 H2O
2 benzyloxycarbonyl-L-alanyl-L-arginine + rhodamine-110
-
specific trypsin substrate
-
-
?
intestinal alkaline sphingomyelinase bound to mucosa + H2O
free intestinal alkaline sphingomyelinase
N-alpha-benzoyl-DL-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-Arg-2-naphthylamide + H2O
N-alpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
-
?
N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-arginine + ethanol
-
-
-
-
?
N-alpha-benzoyl-L-Lys-p-nitroanilide + H2O
N-alpha-benzoyl-L-Lys + p-nitroaniline
-
-
-
-
?
N-benzoyl-DL-arginine 4-nitroanilide + H2O
N-benzoyl-DL-arginine + 4-nitroaniline
-
a synthetic trypsin substrate
-
-
?
p-nitrophenyl-p'-guanidino benzoate + H2O
p-nitrophenol + p-guanidinobenzoate
-
-
-
?
pro-matrix metalloproteinase-2 + H2O
matrix metalloproteinase-2 + pro-peptide
-
activation by trypsin depends on various factors such as the level of exogenously added Ca2+ and Brij-35, temperature, and trypsin concentration. Activation occurs as sequential processing, initially generating an active 62 kDa species followed by successive truncation of the C-terminal domain leading to active species of 56 kDa, 52 kDa and 50kDa. Comparison with activation of pro-matrix metalloproteinase-2 by membrane-type 1 metalloproteinase or 4-aminophenylmercuric acetate
-
-
?
additional information
?
-
-
the active centre is the catalytic triad: His57, Ser195, Asp102
-
-
?
intestinal alkaline sphingomyelinase bound to mucosa + H2O
free intestinal alkaline sphingomyelinase
-
cleavage at R440, first tryptic site upstream of signal anchor. Physiological role of enzyme in sphingomyelin digestion
-
-
?
intestinal alkaline sphingomyelinase bound to mucosa + H2O
free intestinal alkaline sphingomyelinase
-
cleavage at R440, first tryptic site upstream of signal anchor
-
-
?
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
intestinal alkaline sphingomyelinase bound to mucosa + H2O
free intestinal alkaline sphingomyelinase
-
cleavage at R440, first tryptic site upstream of signal anchor. Physiological role of enzyme in sphingomyelin digestion
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bisphenol A
-
the secondary and tertiary structures of trypsin are altered by bisphenol S binding, which results in the loosening of the skeleton of the enzyme. Bisphenol S induces microenvironmental changes around tyrosine and tryptophan residues of trypsin. The activity of trypsin does not change remarkably with the increasing concentration of bisphenol S. The binding of bisphenol S to trypsin is a spontaneous process and hydrogen bonding and hydrophobic interactions play a vital role in stabilizing the bisphenol S-trypsin complex. The binding constants of bisphenol S with trypsin are 74200 (25°C) and 59100 L/mol (37°C)
Ecballium elaterium trypsin inhibitor II
-
EETI, a a model member of the knottin family, used for construction of libraries of EETI loop-substituted variants with diversity in both amino acid sequence and loop length, wild-type EETI or loop-substituted clones expressed from yeast, structure-function analysis, modelling, overview
-
Soybean trypsin inhibitor
-
a Kunitz trypsin inhibitor from soybean seeds, identification of mutants, several polymorphic types that are controlled by multiple alleles, overview. Development of a single nucleotide amplified polymorphism marker for the classification of the predominant KTi types, Tia and Tib, and evaluation of KTi activities by differing KTi type total 451 soybean mutant lines, overview. Trypsin inhibitor type and trypsin inhibitor activity in TIU/mg, overview
-
tissue inhibitor of matrix metalloproteinases-2
-
TIMP-2, prevents the C-terminal truncation of activated metalloproteinase-2, without affecting the generation of the initial 62 kDa activated species
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.06
N-alpha-benzoyl-L-Arg-p-nitroanilide
-
recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C
5.7
N-alpha-benzoyl-L-Lys-4-nitroanilide
-
recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C
1.26
N-alpha-benzoyl-L-arginine ethyl ester
-
in 20 mM TBS (pH 7.6) for 10 min at 25°C, in the absence of sugars or glycoproteins
2.81
N-alpha-benzoyl-L-arginine ethyl ester
-
in 20 mM TBS (pH 7.6) for 10 min at 25°C, in the presence of 0.2 M methyl-alpha-D-galactoside
3.2
N-alpha-benzoyl-L-arginine ethyl ester
-
in 20 mM TBS (pH 7.6) for 10 min at 25°C, in the presence of 0.2 M methyl-alpha-D-mannoside
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.46
N-alpha-benzoyl-L-Arg-p-nitroanilide
-
recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C
0.56
N-alpha-benzoyl-L-Lys-4-nitroanilide
-
recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
vmax-value is 5467 microgramms per min for free enzyme, 793 microgramms per min for immobilized enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
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
malfunction
-
trypsin from pancreatic acinar cells destroys islets. Thus pancreatic slet transplantation which has emerged as an effective therapy and potential cure for type 1 diabetes mellitus, requires inhibition of trypsin activity by ulinastatin or pefabloc, optimization of islet preservation using the two-layer method, TLM, overview
physiological function
-
trypsin activates PAR4 null murine platelets. Trypsin causes shape change without increasing intracellular calcium levels in PAR4 null murine platelets. Trypsin-induced platelet shape change is abolished by either p160ROCK inhibitor, Y27632 or H1152. Trypsin causes phosphorylation of myosin light chain (Thr18), but not Akt or Erk. Trypsin causes a similar shape change in PAR4-desensitized PAR3 null murine platelets as in PAR4 null murine platelets, indicating that trypsin does not activate PAR3 to cause shape change. The Src family kinase inhibitor PP2 abolishes trypsin-induced, but not AYPGKF-induced, shape change
additional information
-
analysis of trypsin immunogenicity in male CBA mice compared to other serine proteases, 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). TRYP_PIG
231
0
24409
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamic simulation to study trypsin with and without a six-aminoacid peptide bound in the solvents water, acetonitrile and hexane. The enzyme is more compact and less native-like in hexane than in the other two polar solvents. The substrate can stabilize the native protein structure in the two polar media, but not in the nonpolar hexane. There are no significant differences in the conformation of the S1 pocket upon the substrate binding in water and acetonitrile media while a reverse behavior is observed in hexane media, implying a possible induced fit binding mechanism in the non-polar media. The substrate binding enhances the stability of catalytic H-bond network. The enzyme and the substrate appear to be more appropriate to the reactive conformation in the organic solvents compared with aqueous solution. There is much greater substrate binding strength in hexane media than the water and acetonitrile ones
sitting drop vapor diffusion method. Crystals of porcine trypsin are prepared with either a vacant S1-subsite or with the S1-subsite occupied by one of three alcohols, slected for their properties as substrate analogues: guanidine-3-propanol, 4-aminobutanol and p-hydroxymethylbenzamidine
enzyme in complex with Tamarindus indica trypsin inhibitor, sitting drop vapour diffusion method, at 20°C, mixing of 0.002 ml of 5 mg/ml protein solution with 0.002 ml of precipitant solution containing 4 M ammonium acetate and 0.1 M sodium acetate trihydrate, pH 4.6, X-ray diffraction structure determination and analysis at 2.0 A resolution, presence of one unit of inhibitor-trypsin complex per asymmetric unit
-
in complex with heterochiral peptide t-butyloxycarbonyl-L-Pro-D-Asp-alpha-methyl-alanyl-L-Leu-L-Ala-NHMe. Peptide does not bind at active site but is located in the interstitial region, and interacts with the calcium-binding loop
-
sitting-drop vapour diffusion method, crystals of beta-trypsin-bdellastasin complex. Deamination, isomerization and racemization of Asn115 is the key step in crystallization
-
vapour-diffusion hanging-drop technique, crystal structures of trypsin in presence of varying concentrations of polydocanol. Polydocanol binds to the protein with its hydrophilic head. There are at least 11 binding sites for polydocanol in trypsin. The hydrophilic binding of polydocanol results in cross-linked pairs of trypsin molecules
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80 - 130
-
dehydration occurs at 80-130°C with a loss of both water and activity, the activity decreases significantly above 130°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enhancement of stability and aggregation of proteins in the presence of low concentrations of polydocanol
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetonitrile
molecular dynamic simulation to study trypsin with and without a six-aminoacid peptide bound in the solvents water, acetonitrile and hexane. The enzyme is more compact and less native-like in hexane than in the other two polar solvents. The substrate can stabilize the native protein structure. There are no significant differences in the conformation of the S1 pocket upon the substrate binding in water and acetonitrile media. The substrate binding enhances the stability of catalytic H-bond network. The enzyme and the substrate appear to be more appropriate to the reactive conformation in the organic solvents compared with aqueous solution
hexane
molecular dynamic simulation to study trypsin with and without a six-aminoacid peptide bound in the solvents water, acetonitrile and hexane. The enzyme is more compact and less native-like in hexane than in the other two polar solvents. The substrate cannot stabilize the native protein structure in the nonpolar hexane. There are no significant differences in the conformation of the S1 pocket upon the substrate binding in water and acetonitrile media while a reverse behavior is observed in hexane media, implying a possible induced fit binding mechanism in the non-polar media. The substrate binding enhances the stability of catalytic H-bond network. The enzyme and the substrate appear to be more appropriate to the reactive conformation in the organic solvents compared with aqueous solution. There is much greater substrate binding strength in hexane media than the water and acetonitrile ones
acetonitrile
-
the presence of organic cosolvents like acetonitrile decreases the ability of boiling to completely quench trypsin activity
guanidine-HCl
-
the recombinant enzyme retains about 40 and 20% activity in 0.1 and 0.3 M guanidine-HCl
urea
-
the recombinant enzyme retains approximately 50 and 20% of its activity in 2 and 4 M urea, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
dental plaque is a causative factor for oral disease and a potential reservoir for respiratory infection in the elderly. Therefore, there is a critical need for the development of effective methods to remove oral biofilm. Proteases reduce oral biofilm in vivo in elderly subjects. Tablets containing actinidin remove tongue coating in elderly subjects. Oral Actinomyces biofilm is significantly reduced by the proteases papain, actinidin and trypsin. Papain and trypsin effectively digest the major fimbrial proteins, FimP and FimA, from Actinomyces. Actinidin, papain and trypsin reduce multispecies biofilm that is reconstructed in vitro. Papain and trypsin inhibit formation of multispecies biofilm in vitro
biotechnology
-
enzyme molecules are associated with the outer protein layer of rotavirus virions propagated in cell culture medium containing the enzyme. Enzyme is present only in triple-layer particles, not in double-layer particles. Enzyme associated with virions is inactive, activity is recovered only when the outer capsid is solubilized. Incorporation of trypsin into rotavirus particles may enhance its infectivity
synthesis
synthesis
-
production of human insulin-threonine-ester, which can be simply converted into human insulin by hydrolysis with subsequent purification steps
synthesis
-
covalent immobilization of enzyme onto poly(methyl methacrylate)-co-(ethyl acrylate)-co-(acrylic acid) latex particles. Immobilized enzyme shows higher optimal temperature and pH-value than free form. Immobilized enzyme exhibits higher KM-value than free form and better chemical and thermal stability, it maintains 63% of initial activity after reusing ten times
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walker, J.E.; Keil, B.
Purification and characterisation of different active forms of pork trypsin
Eur. J. Biochem.
32
486-491
1973
Sus scrofa
Johnson, A.; Gautham, N.; Pattabhi, V.
Crystal structure at 1.63 A resolution of the native form of porcine beta-trypsin: revealing an acetate ion binding site and functional water network
Biochim. Biophys. Acta
1435
7-21
1999
Sus scrofa
Jeohn, G.H.; Serizawa, S.; Iwamatsu, A.; Takahashi, K.
Isolation and characterization of gastric trypsin from the microsomal fraction of porcine gastric antral mucosa
J. Biol. Chem.
270
14748-14755
1995
Sus scrofa
Huang, Q.; Wang, Z.; Li, Y.; Liu, S.; Tang, Y.
Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin
Biochim. Biophys. Acta
1209
77-82
1994
Sus scrofa
Rester, U.; Moser, M.; Huber, R.; Bode, W.
L-Isoaspartate 115 of porcine beta-trypsin promotes crystallization of its complex with bdellastasin
Acta Crystallogr. Sect. D
56
581-588
2000
Sus scrofa
-
Deepthi, S.; Johnson, A.; Pattabhi, V.
Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol
Acta Crystallogr. Sect. D
57
1506-1512
2001
Sus scrofa
Schimoler-O'Rourke, R.; Richardson, M.; Selitrennikoff, C.P.
Zeamatin inhibits trypsin and alpha-amylase activities
Appl. Environ. Microbiol.
67
2365-2366
2001
Sus scrofa
Transue, T.R.; Krahn, J.M.; Gabel, S.A.; DeRose, E.F.; London, R.E.
X-ray and NMR characterization of covalent complexes of trypsin, borate, and alcohols
Biochemistry
43
2829-2839
2004
Sus scrofa (P00761), Sus scrofa
Ladisch, M.R.; Kohlmann, K.L.
Recombinant human insulin
Biotechnol. Prog.
8
469-478
1992
Sus scrofa
Wu, J.; Liu, F.; Nilsson, A.; Duan, R.D.
Pancreatic trypsin cleaves intestinal alkaline sphingomyelinase from mucosa and enhances the sphingomyelinase activity
Am. J. Physiol. Gastrointest. Liver Physiol.
287
G967-G973
2004
Sus scrofa
Shamaladevi, N.; Pattabhi, V.
Secondary binding site of trypsin: revealed by crystal structure of trypsin-peptide complex
J. Biomol. Struct. Dyn.
22
635-642
2005
Sus scrofa
Benureau, Y.; Huet, J.C.; Charpilienne, A.; Poncet, D.; Cohen, J.
Trypsin is associated with the rotavirus capsid and is activated by solubilization of outer capsid proteins
J. Gen. Virol.
86
3143-3151
2005
Sus scrofa
Lindstad, R.I.; Sylte, I.; Mikalsen, S.O.; Seglen, P.O.; Berg, E.; Winberg, J.O.
Pancreatic trypsin activates human promatrix metalloproteinase-2
J. Mol. Biol.
350
682-698
2005
Sus scrofa
Kang, K.; Kan, C.; Yeung, A.; Liu, D.
The properties of covalently immobilized trypsin on soap-free P(MMA-EA-AA) latex particles
Macromol. Biosci.
5
344-351
2005
Sus scrofa
Finehout, E.J.; Cantor, J.R.; Lee, K.H.
Kinetic characterization of sequencing grade modified trypsin
Proteomics
5
2319-2321
2005
Sus scrofa
Takekawa, H.; Ina, C.; Sato, R.; Toma, K.; Ogawa, H.
Novel carbohydrate-binding activity of pancreatic trypsins to N-linked glycans of glycoproteins
J. Biol. Chem.
281
8528-8538
2006
Bos taurus, Sus scrofa
Mayoral, J.G.; Alarcon, F.J.; Martinez, T.F.; Barranco, P.; Noriega, F.
An improved end-point fluorimetric procedure for the determination of low amounts of trypsin activity in biological samples using rhodamine-110-based substrates
Appl. Biochem. Biotechnol.
160
1-8
2009
Sus scrofa
Otsuka, M.; Fukui, Y.; Ozaki, Y.
Comparative evaluation of bioactivity of crystalline trypsin for drying by Fourier-transformed infrared spectroscopy
Colloids Surf. B Biointerfaces
69
194-200
2009
Sus scrofa
Sun, Y.; Chen, M.Y.; Zhao, C.; An, K.N.; Amadio, P.C.
The effect of hyaluronidase, phospholipase, lipid solvent and trypsin on the lubrication of canine flexor digitorum profundus tendon
J. Orthop. Res.
26
1225-1229
2008
Sus scrofa
Kiser, J.Z.; Post, M.; Wang, B.; Miyagi, M.
Streptomyces erythraeus trypsin for proteomics applications
J. Proteome Res.
8
1810-1817
2009
Sus scrofa, Saccharopolyspora erythraea (Q54137), Saccharopolyspora erythraea
Petritis, B.; Qian, W.J.; Camp, D.; Smith, R.
A simple procedure for effective quenching of trypsin activity and prevention of 18O-labeling back-exchange
J. Proteome Res.
8
2157-2163
2009
Sus scrofa
Zhang, B.; Wang, D.F.; Fan, Y.; Zhang, L.; Luo, Y.
Affinity purification of trypsin inhibitor with anti-Aspergillus flavus activity from cultivated and wild soybean
Mycopathologia
167
163-171
2009
Sus scrofa
Mattson, K.J.; Devlin, B.R.; Loskutoff, N.M.
Comparison of a recombinant trypsin with the porcine pancreatic extract on sperm used for the in vitro production of bovine embryos
Theriogenology
69
724-727
2008
Bos taurus, Sus scrofa
Wee, Y.M.; Kim, S.C.; Koo, S.K.; Kim, Y.H.; Jung, E.J.; Choi, M.Y.; Park, Y.H.; Park, K.T.; Lim, D.G.; Han, D.J.
Improved islet yields after purification following the novel endogenous trypsin inhibitor and histidine-tryptophan-ketoglutarate treatment in pigs
Transplant. Proc.
40
2585-2587
2008
Sus scrofa
Tomar, S.; Patil, D.N.; Datta, M.; Tapas, S.; Preeti, S.; Chaudhary, A.; Sharma, A.K.; Tomar, S.; Kumar, P.
Crystallization and preliminary X-ray diffraction analysis of the complex of Kunitz-type tamarind trypsin inhibitor and porcine pancreatic trypsin
Acta Crystallogr. Sect. F
65
1179-1181
2009
Sus scrofa
Noguchi, H.; Ueda, M.; Hayashi, S.; Kobayashi, N.; Okitsu, T.; Iwanaga, Y.; Nagata, H.; Liu, X.; Kamiya, H.; Levy, M.F.; Matsumoto, S.
Comparison of trypsin inhibitors in preservation solution for islet isolation
Cell Transplant.
18
541-547
2009
Sus scrofa
Lahti, J.; Silverman, A.; Cochran, J.
Interrogating and predicting tolerated sequence diversity in protein folds: Application to E. elaterium trypsin inhibitor-II cystine-knot miniprotein
PLoS Comput. Biol.
5
e1000499
2009
Sus scrofa
Darani, H.Y.; Doenhoff, M.J.
Anomalous immunogenic properties of serine proteases
Scand. J. Immunol.
70
384-388
2009
Sus scrofa
Kim, D.S.; Lee, K.J.; Kim, J.B.; Kim, S.H.; Song, J.Y.; Seo, Y.W.; Lee, B.M.; Kang, S.Y.
Identification of Kunitz trypsin inhibitor mutations using SNAP markers in soybean mutant lines
Theor. Appl. Genet.
121
751-760
2010
Sus scrofa
Wang, Y.Q.; Zhang, H.M.
Effects of bisphenol S on the structures and activities of trypsin and pepsin
J. Agric. Food Chem.
62
11303-11311
2014
Sus scrofa
Meng, Y.; Yuan, Y.; Zhu, Y.; Guo, Y.; Li, M.; Wang, Z.; Pu, X.; Jiang, L.
Effects of organic solvents and substrate binding on trypsin in acetonitrile and hexane media
J. Mol. Model.
19
3749-3766
2013
Sus scrofa (P00761)
Mao, Y.; Kunapuli, S.P.
Trypsin causes platelet activation independently of known protease-activated receptors
Thromb. Haemost.
110
1241-1249
2013
Sus scrofa
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