CHY5S

αα-Chymotrypsin aus Rinderpankreas

≥40 units/mg protein, vial of 5 mg

• Synonym(e): α-chymotrypsin A and B
• CAS-Nummer: 9004-07-3
• UNSPSC Code: 12352204
• NACRES: NA.54
• EC Number: 232-671-2
• MDL number: MFCD00130481
• EG-Nummer: 3.4.21.1 (BRENDA, IUBMB)
• eCl@ss: 42010112
• Specific activity: ≥40 units/mg protein
• Biological source: bovine pancreas

Eigenschaften

• biological source: bovine pancreas
• Quality Segment: 200
• description: aseptically filled
• type: Type IV-S
• form: solid
• specific activity: ≥40 units/mg protein
• mol wt: 25 kDa
• composition: protein, ≥85% UV
• packaging: vial of 5 mg
• UniProt accession no.: P00767
• storage temp.: −20°C
• Gene Information: cow ... CTRB1(618826)

Beschreibung

Application

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.

The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration.[1]

α-Chymotrypsin from bovine pancreas has been used:

• as a supplement for the collection of semen into Tris diluent
• as one of the proteases in the analysis of major histocompatibility complex (MHC) class II protease sensitivity assay
• as a component in YEPD broth for biofilm dispersion assay
• in the preparation of chitinase–chymotrypsin–DMSO buffer (CCD buffer) for enzymatic digestion of larvae

Biochem/physiol Actions

Ein Serin-Protease, die Peptidbindungen mit aromatischen oder großen hydrophoben Seitenketten (Tyr, Trp, Phe, Met, Leu) am Carboxylende der Bindung hydrolysiert.

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, and α2-macroglobulin, 10 mM Cu²⁺ and Hg^2+.

Analysis Note

Protein determined by A1%/280

Other Notes

Eine Einheit hydrolysiert 1.0 μmol BTEE pro min bei pH 7.8 und 25 °C.

Sicherheitshinweise

• pictograms: GHS08,GHS07,GHS09
• signalword: Danger
• hcodes: H302,H315,H319,H334,H335,H400
• pcodes: P261 - P264 - P273 - P301 + P312 - P302 + P352 - P305 + P351 + P338
• Hazard Classifications: Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
• target_organs: Respiratory system
• Lagerklasse: 11 - Combustible Solids
• wgk: WGK 1
• ppe: dust mask type N95 (US), Eyeshields, Faceshields, Gloves