| Identification | Back Directory | [Name]
Chymotrypsin | [CAS]
9004-07-3 | [Synonyms]
chymar
ec3445
ec3446
enzeon
impral
quimar
zolyse
zolyes
D03484
kimoral
avazyme
catarase
chymozym
kimopsin
alfapsin
zonulsin
Alpapsin
chymetin
3xcryst.
chymolase
chymotest
quimotrase
EC 3.4.21.1
alphachymar
e.c.3.4.4.5
e.c.3.4.4.6
EC: 3.4.21.1
CHYMOTRYPSIN
CHYMOTRIPSIN
Catarase (tn)
IUB: 3.4.21.1
chymotrypsinb
CHYMOTRYPSIN A
D-CHYMOTRYPSIN
A-CHYMOTRYPSIN
BETA-CHYMOTRYPSIN
TLCK-CHYMOTRYPSIN
alpha-chymarophth
ALPHA-CHYMOTRYPSIN
CHYMOTRYPSIN I USP
CHYMOTRYPSIN, ALPHA
Chymotrypsin (300 mg)
A-chymotrypsin type vi
recombinant chymotrypsin
Chymotrypsin (jan/usp/inn)
ALPHA-CHYMOTRYPSIN TYPE VI
ALPHA-CHYMOTRYPSIN TYPE VII
ALPHA-CHYMOTRYPSIN TYPE I-S
α-chymotrypsin, tlck treated
alpha-Chymotrypsin, USP grade
CHYMOTRYPSIN, BOVINE PANCREAS
a-Chymotrypsin, Bovine Pancreas
A-chymotrypsin sequencing grade
alpha-ChyMotrypsin,ChyMotrypsin
ALPHA-CHYMOTRYPSIN, TLCK TREATED
ALPHA-CHYMOTRYPSIN BOVINE PANCREAS
Gamma-ChymotrypsinExBovinePancreas
α-chymotrypsin from human pancreas
A-chymotrypsin from human pancreas
Alpha-ChyMotrypsin 3x crystallized
sequencing recombinant chymotrypsin
B-CHYMOTRYPSIN FROM BOVINE PANCREAS
alpha-chymotrypsinfrombovinepancreas
beta-Chymotrypsin from Bovine Pancreas
alpha-chymotrypsin fr.bov.pancr.free of
A-chymotrypsin type ii from bovine*pancreas
A-chymotrypsin type I-S from bovine*pancreas
ChyMotrypsin(bovine)/ α-ChyMotrypsin(bovine)
Chymotrypsin (300 mg) (COLD SHIPMENT REQUIRED)
ALPHA-CHYMOTRYPSIN FROM BOVINE PANCREAS, 25 UG
α-Chymotrypsin-Agarose from bovine pancreas
Chymotrypsin from bovine pancreas min. 40 U/mg
α-chymotrypsin tlck treated from bovine pancreas
gamma-chymotrypsin type ii: from*bovine pancreas
α-ChyMotrypsin froM bovine pancreas(TLCK Treated)
α-Chymotrypsin–acrylic beads from bovine pancreas
ALPHA-CHYMOTRYPSIN FROM BOVINE PANCREAS, ~50 U/MG
α-ChyMotrypsin, froM bovine pancreas, 1000 units/Mg
α-Chymotrypsin, Inactivated from bovine pancreas
ChyMotrypsin froM bovine pancreas Min. 40 U/Mg powder
a-Chymotrypsin from bovine pancreas from bovine pancreas
ALPHA-CHYMOTRYPSIN FROM BOVINE PANCREAS LYO. PWD. ~60 U/MG
ALPHA-CHYMOTRYPSIN TLCK TREATED LYOPH. 6 0 U/MG WHITE POWD.
ALPHA-CHYMOTRYPSIN FR.BOV.PANCR.FREE OF LOW MOL.WGHT.PEP.FR
?-Chymotrypsin, USP Grade alpha-Chymotryspsin, Bovine, USP Grade
α-Chymotrypsin Insoluble enzyme attached to carboxymethyl cellulose from bovine pancreas
α-ChyMotrypsin froM Bovine Pancreas (3× recrystallized, salt free froM 20% Ethanol, presence of CalciuM enhances its activity and stability)
beta-Chymotrypsin from Bovine Pancreas (3* recrystallized, salt free from 20% Ethanol, presence of Calcium enhances its activity and stability)
alpha-Chymotrypsin from Bovine Pancreas (3* recrystallized, salt free from 20% Ethanol, presence of Calcium enhances its activity and stability) | [EINECS(EC#)]
232-671-2 | [Molecular Formula]
N/A | [MDL Number]
MFCD00130481 |
| Chemical Properties | Back Directory | [Appearance]
Lyophilized powder, dialyzed | [Melting point ]
127°C | [density ]
1.37[at 20℃] | [vapor pressure ]
0Pa at 25℃ | [storage temp. ]
2-8°C
| [solubility ]
Reconstitute in 1mM HCl. Soluble at 10mg/ml in 1mM HCl. 2mM calcium chloride serves as a stabilizer. Store aliquoted solutions at -20°C for up to a week. | [form ]
salt-free, lyophilized powder
| [color ]
white
| [biological source]
human pancreas | [Water Solubility ]
125g/L at 25℃ | [Merck ]
13,2282 | [Specific Activity]
2,000-3,500units/g agarose (One ml gel will yield 65-120units) | [Cosmetics Ingredients Functions]
SKIN CONDITIONING | [LogP]
-1.3 at 20℃ | [EPA Substance Registry System]
Chymotrypsin(9004-07-3) |
| Hazard Information | Back Directory | [Chemical Properties]
Lyophilized powder, dialyzed | [Usage]
α-Chymotrypsin from bovine has been used in a study to inform proteasome inhibition in order to advance anticancer research. α-Chymotrypsin from bovine has also been used in a study that functionalized surface anchored poly(methylhydrosiloxane) thin films on oxidized silicon wafers. | [Uses]
α-Chymotrypsin from bovine has been used in a study to inform proteasome inhibition in order to advance anticancer research. α-Chymotrypsin from bovine has also been used in a study that functionalized surface anchored poly(methylhydrosiloxane) thin films on oxidized silicon wafers. | [General Description]
Chymotrypsin (Chymar) is extractedfrom mammalian pancreas and is used in cataractsurgery. A dilute solution is used to irrigate the posteriorchamber of the eye to dissolve the fine filaments that holdthe lens. | [Biochem/physiol Actions]
α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. Its pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, α2-macroglobulin, 10 mM Cu2+ and Hg2+. | [Mechanism of action]
The general mechanism for chymotrypsin is the classic serine protease mechanism. Hydrolytic proteolysis by α-chymotrypsin begins with an initial nucleophilic attack on the peptide bond by Ser 195, activated by deprotonation by His 57. This leads to forming a tetrahedral intermediate, stabilized by the amide groups of Ser 195 and Gly 193. The subsequent collapse of this intermediate, assisted by protonation of the leaving group by His 57 and Asp 102, leads to an acyl-enzyme intermediate. Activation of a water molecule by His 57 and Asp 102 facilitates hydrolysis of this intermediate, resulting in the reformation of the catalytically active serine residue and the release of the product facilitated by protonation with His 57. | [Purification Methods]
α-Chymotrypsin is crystallised twice from four-tenths saturated ammonium sulfate solution, then dissolved in 1mM HCl and dialysed against 1mM HCl at 2-4o. The solution is stored at 2o [Lang et al. J Am Chem Soc 80 4923 1958]. | [References]
[1] R J Schilling, A K Mitra. “Degradation of insulin by trypsin and alpha-chymotrypsin.” Pharmaceutical Research 8 6 (1991): 721–7.
|
| Questions And Answer | Back Directory | [Degradation]
The rate and extent of insulin degradation by trypsin and α-Chymotrypsin were examined in vitro, and the initial sites of cleavage by α-Chymotrypsin were identified. The apparent Km for both enzymes was approximately the same, but the apparent Vmax for α-Chymotrypsin was 8.6 times greater. At a molar ratio of 172:1 (insulin: enzyme), chymotrypsin caused near-total loss of insulin within 40 min, while very little insulin was degraded by trypsin. Chymotrypsin appeared to cleave initially at the carboxyl side of the B26-Tyr and A19-Tyr residues, and additional cleavage at the B16-Tyr, B25-Phe, and A14-Tyr residue sites also occurred rapidly. Only two to three other susceptible bonds, which are not exposed at the surface of the insulin molecule, remained intact after the quenching of initial cleavage[1].
|
|
| Company Name: |
J & K SCIENTIFIC LTD.
|
| Telephone: |
18210857532 18210857532 |
| Website: |
https://www.jkchemical.com |
| Company Name: |
Energy Chemical
|
| Telephone: |
400-0056266 |
| Website: |
www.energy-chemical.com |
| Company Name: |
China Langchem Inc.
|
| Telephone: |
0086-21-58956006 |
| Website: |
www.chemicalbook.com/ShowSupplierProductsList19141/0_EN.htm |
|