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CHY5S

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

≥40 units/mg protein, vial of 5 mg

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Synonym(s):
α-chymotrypsin A and B
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

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.

storage temp.

−20°C

Gene Information

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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.
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

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

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, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.

Unit Definition

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Analysis Note

Protein determined by A1%/280

signalword

Danger

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

wgk_germany

WGK 1

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


Certificates of Analysis (COA)

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A triad of molecular regions contribute to the formation of two distinct MHC class II conformers
Drake L A and Drake J R
Molecular Immunology, 74, 59-70 (2016)
MrkD (1P) from Klebsiella pneumoniae IA565 allows for co-existence with Pseudomonas aeruginosa and protection from protease-mediated biofilm detachment
Childers B M, et al.
Infection and Immunity, 74, IAI-00521 (2013)
Effect of enzyme treatment and mechanical removal of alpaca (Vicugna pacos) seminal plasma on sperm functional integrity
Morton K M, et al.
JOURNAL-SHANDONG UNIVERSITY OF SCIENCE AND TECHNOLOGY NATURAL SCIENCE, 5, 62-81 (2012)
K L Honea et al.
Journal of assisted reproduction and genetics, 10(4), 255-260 (1993-05-01)
This study was designed to assess the impact of limited proteolysis with alpha-chymotrypsin on the sperm penetration assay (SPA) of infertile patients and to identify a group whose results would normalize with this pretreatment. Further, the application of this treatment
Immunofluorescent antibody staining of intact Drosophila larvae
Manning L and Doe C Q
Nature Protocols, 12(1), 1-1 (2017)

Protocols

Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.

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