CAS 9035-75-0
:Chymotrypsinogen
Description:
Chymotrypsinogen is a serine protease enzyme precursor, primarily produced in the pancreas. It is classified as a zymogen, meaning it is an inactive form that requires activation to become functional. Upon entering the small intestine, chymotrypsinogen is converted into its active form, chymotrypsin, through the action of the enzyme trypsin. This activation involves the cleavage of specific peptide bonds, resulting in a conformational change that allows chymotrypsin to perform its enzymatic function. Chymotrypsin plays a crucial role in the digestive process by breaking down proteins into smaller peptides and amino acids, facilitating nutrient absorption. The enzyme exhibits specificity for aromatic amino acids, such as phenylalanine, tryptophan, and tyrosine. Chymotrypsinogen is a glycoprotein, and its structure includes multiple disulfide bonds that stabilize its conformation. It is important in both physiological and pathological processes, and its activity can be influenced by various factors, including pH and the presence of inhibitors. Understanding chymotrypsinogen is essential in biochemistry and medicine, particularly in the context of digestive health and enzyme regulation.
Formula:Unspecified
Synonyms:- Chymotrypsinogen A
- Chymotrypsinogen (crystal
- Chymotrypsinogen
- Chymotrypsinogen B
- Chymotrypsinogene
- Quimotripsinogeno
- α-Chymotrypsinogen
- α-Chymotrypsinogen A
- MeSH ID: D002919
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Found 3 products.
Chymotrypsinogen
CAS:Chymotrypsinogen is an inactive precursor of Chymotrypsin . Chymotrypsin is a serine protease produced by the pancreas [1] [2] .Color and Shape:Solida-Chymotrypsinogen A (5x cryst) ex. Bovine Pancreas, 45U/mg protein
CAS:Color and Shape:White to off white, Powderα-Chymotrypsinogen A from bovine pancreas
CAS:α-Chymotrypsinogen A is a protein that functions as an enzyme inhibitor. It is a basic protein with an amino acid sequence that is similar to trypsinogen A, and it has been used as a model protein for studying the effects of metal ions on proteins. α-Chymotrypsinogen A can be found in the pancreas of bovines. α-Chymotrypsinogen A is also used as a reagent in analytical chemistry for detecting chloride, metal chelate, and solute. The chloride ion binds to α-chymotrypsinogen A due to its positive charge, which causes the redox potential of the molecule to increase. This leads to hydrogen bonding between the chloride ion and trehalose molecules on the surface of α-chymotrypsinogen A. When metal ions are added, they bind to basic groups on the protein's surface and form complexes that have different redoxPurity:Min. 95%
