The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa.This information and the basic structure description of the enzyme can be found on our product information sheet (under Documents, above) at our website.
C3142
α-Chymotrypsin from bovine pancreas
(TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein
Sinónimos:
TLCK-Chymotrypsin
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About This Item
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Nivel de calidad
tpo
Type VII
Formulario
essentially salt-free, lyophilized powder
actividad específica
≥40 units/mg protein
mol peso
25 kDa
solubilidad
1 mM HCl: soluble 10 mg/mL, clear
Nº de acceso UniProt
temp. de almacenamiento
−20°C
Información sobre el gen
cow ... CTRB1(618826)
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Aplicación
α-Chymotrypsin from Sigma has been used to determine the crystal structures of two homologous inhibitors (pars intercerebralis major peptide-C and pars intercerebralis major peptide-D2v) from the insect Locusta migratoria by forming a complex with the enzyme.[1]
Acciones bioquímicas o fisiológicas
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+.
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.
Definición de unidad
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
Nota de preparación
TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.
Nota de análisis
Protein determined by A1%/280
Otras notas
View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer
Inhibidor
Referencia del producto
Descripción
Precios
sustrato
Referencia del producto
Descripción
Precios
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Órganos de actuación
Respiratory system
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Equipo de protección personal
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Certificados de análisis (COA)
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Los clientes también vieron
M Gestin et al.
Digestive diseases and sciences, 42(6), 1302-1311 (1997-06-01)
A specific method for pancreatic elastase II activity analysis was developed. True elastase II activity could be discriminated from that of elastase I and chymotrypsin. The postnatal development of four pancreatic proteases in the duodenal juice of children and in
Zhenyao Luo et al.
FEBS letters, 592(13), 2341-2350 (2018-06-02)
The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn2+ for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn2+ homeostasis. However, the mechanistic basis
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Actin polymerization generates forces for cellular processes throughout the eukaryotic kingdom, but our understanding of the 'ancient' actin turnover machineries is limited. We show that, despite > 1 billion years of evolution, pathogenic Leishmania major parasite and mammalian actins share the same
A Roussel et al.
The Journal of biological chemistry, 276(42), 38893-38898 (2001-08-10)
The crystal structures of two homologous inhibitors (PMP-C and PMP-D2v) from the insect Locusta migratoria have been determined in complex with bovine alpha-chymotrypsin at 2.1- and 3.0-A resolution, respectively. PMP-C is a potent bovine alpha-chymotrypsin inhibitor whereas native PMP-D2 is
Tobias Koschubs et al.
Nucleic acids research, 38(10), 3186-3195 (2010-02-04)
Mediator is the central coactivator complex required for regulated transcription by RNA polymerase (Pol) II. Mediator consists of 25 subunits arranged in the head, middle, tail and kinase modules. Structural and functional studies of Mediator are limited by the availability
Artículos
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
Protocolos
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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What is the molecular weight of alpha-chymotrypsin from bovine pancreas (Product No. C3142)?
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How can solutions of alpha-chymotrypsin (Product No. C3142) be stored?
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Stock solutions prepared in 1 mM HCl, containing 2 mM calcium chloride, can be stored at -20 ° for about one week.
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How do you recommend preparing a solution of Product No. C3142?
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It is recommended to reconstitute Product No. C3142 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as both a stabilizer (and possibly an activator) of the enzyme.
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What is the Department of Transportation shipping information for this product?
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Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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What is the pH optimum for the enzyme, Product No. C3142?
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The pH optimum for alpha-chymotrypsin is between pH 7.5-8.5. Please see the following reference: Wilcox, P.E., Chymotrypsingogens-chymotrypsins, Methods in Enzymology, 19, 64-80 (1970).
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