9035-75-0

Basic information

• Product Name: CHYMOTRYPSINOGEN A
• Synonyms: ALPHA-CHYMOTRYPSIN TYPE II;CHYMOTRYPSINOGEN;CHYMOTRYPSINOGEN A;CHYMOTRYPSINOGEN A, BOVINE;EC 3.4.21.1;A-chymotrypsinogen A type ii from*bovine pancreas;Chymotrypsinogen (crystal;ChymotrypsinogenAExBovinePancreas
• CAS NO: 9035-75-0
• Molecular Formula: NULL
• Molecular Weight: 0
• EINECS: 232-905-3
• Product Categories: Mass Spectrometry;Peptide and protein standards for mass spectrometry analysisApplication Index;Proteases;Proteases&Protein Sequencing;Proteomics
• Mol File: 9035-75-0.mol
• Article Data: 0

Chemical Properties

• Appearance: /essentially salt-free, lyophilized powder
• Storage Temp.: −20°C
• Solubility: Soluble in 0.001M HCl.
• CAS DataBase Reference: CHYMOTRYPSINOGEN A(CAS DataBase Reference)
• NIST Chemistry Reference: CHYMOTRYPSINOGEN A(9035-75-0)
• EPA Substance Registry System: CHYMOTRYPSINOGEN A(9035-75-0)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• Hazardous Substances Data: 9035-75-0(Hazardous Substances Data)

Usage

Description

Chymotrypsinogen A, derived from bovine pancreas, is a zymogen that contains 5 disulfide bridges and has an isoelectric pH of 8.97. It serves as a precursor to the serine protease enzyme, chymotrypsin, which is involved in the hydrolysis of peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the peptide bond.

Uses

Used in Biochemistry Research:
Chymotrypsinogen A is used as a model protein for crystallization reproducibility studies, providing valuable insights into protein structure and function.
Used in Analytical Techniques:
Chymotrypsinogen A is used in the non-invasive determination of solid-state protein conformation using near-infrared (NIR) spectroscopy, allowing for the study of protein behavior under various conditions.
Used in Protein Partitioning Studies:
Chymotrypsinogen A has been utilized to study the partitioning of proteins in polymer/polymer aqueous two-phase systems, contributing to the understanding of protein-polymer interactions.
Used in Self-Interaction Chromatography:
Chymotrypsinogen A is employed in self-interaction chromatography applications, where the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution, aiding in the rapid measurement of protein osmotic second virial coefficients.
Used in Mass Spectrometry Studies:
α-Chymotrypsinogen A from bovine pancreas has been used in the hydrolysis of α-gliadins prior to mass spectroscopy studies, facilitating the analysis of these proteins.

Biochem/physiol Actions

Chymotrypsinogen A requires limited proteolysis for its activation. Chymotrypsinogen A may be activated by trypsin and chymotrypsin (autolytic activation) to form m α, β, γ, δ and π chymotrypsin (depending upon the conditions of activation). Chymotrypsin is a protease that will preferentially cleave peptides on the carboxyl side of aromatic amino acids including tryptophan, tyrosine, and phenylalanine. It will also hydrolyze peptides on the carboxyl side of leucine, methionine, and alanine.