Chymotrypsin

Bezeichnung:Chymotrypsin

CAS-Nr9004-07-3

Englisch Name:α-Chymotrypsin

CBNumberCB4167554

SummenformelN/A

Molgewicht0

MOL-DateiMol file

Synonyma

Chymotrypsin

Chymotrypsin physikalisch-chemischer Eigenschaften

Schmelzpunkt	127°C
Dichte	1.37[at 20℃]
Dampfdruck	0Pa at 25℃
storage temp.	-20°C
Löslichkeit	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.
Aggregatzustand	salt-free, lyophilized powder
Farbe	white
Wasserlöslichkeit	125g/L at 25℃
Merck	13,2282
LogP	-1.3 at 20℃
EPA chemische Informationen	Chymotrypsin (9004-07-3)

Sicherheit

Kennzeichnung gefährlicher	Xn,B
R-Sätze:	36/37/38-42/43-42
S-Sätze:	26-36-36/37-24-22
WGK Germany	3
RTECS-Nr.	GC3050000
F	3-10
TSCA	Yes
HS Code	35079090
Giftige Stoffe Daten	9004-07-3(Hazardous Substances Data)

Gefahreninformationscode (GHS)

α-Chymotrypsin Chemische Eigenschaften,Einsatz,Produktion Methoden

R-Sätze Betriebsanweisung:
R36/37/38:Reizt die Augen, die Atmungsorgane und die Haut.
R42/43:Sensibilisierung durch Einatmen und Hautkontakt möglich.
R42:Sensibilisierung durch Einatmen möglich.
S-Sätze Betriebsanweisung:
S26:Bei Berührung mit den Augen sofort gründlich mit Wasser abspülen und Arzt konsultieren.
S36:DE: Bei der Arbeit geeignete Schutzkleidung tragen.
S36/37:Bei der Arbeit geeignete Schutzhandschuhe und Schutzkleidung tragen.
S24:Berührung mit der Haut vermeiden.
S22:Staub nicht einatmen.
Chemische Eigenschaften
Lyophilized powder, dialyzed
Verwenden
The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration.
Verwenden
α-Chymotrypsin from bovine pancreas has been used in a study to investigate protein extraction by Winsor-III microemulsion systems. α-Chymotrypsin from bovine pancreas has also been used in a study to investigate a new specific fullerene-based fluorescent probe for trypsin.
Verwenden
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.
Allgemeine Beschreibung
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.
läuterung methode
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].
Einzelnachweise
[1] R J Schilling, A K Mitra. “Degradation of insulin by trypsin and alpha-chymotrypsin.” Pharmaceutical Research 8 6 (1991): 721–7.

α-Chymotrypsin Upstream-Materialien And Downstream Produkte

Chymotrypsin Anbieter Lieferant Produzent Hersteller Vertrieb Händler.

9004-07-3, α-Chymotrypsin Verwandte Suche:

Send Inquriy