C9268

Carboxypeptidase A from bovine pancreas

(Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution

• Synonym(s): Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase
• CAS Number: 11075-17-5
• Enzyme Commission number: 3.4.17.1 (BRENDA, IUBMB)
• MDL number: MFCD00130718
• UNSPSC Code: 12352204
• NACRES: NA.54

Properties

• grade: Proteomics Grade
• form: ready-to-use solution
• quality: (Type II-PMSF treated)
• specific activity: ≥50 units/mg protein
• mol wt: ~35 kDa
• purified by: 2× crystallization
• impurities: ≤0.05 BTEE units/mg protein chymotrypsin; ≤10 BAEE units/mg protein trypsin
• storage temp.: 2-8°C

Description

Application

Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been used in a study to investigate the isolation and partial characterization of precursor forms of ostrich carboxypeptidase.

The enzyme from Sigma has been used as a comparison to study the specificity of Metarhizium anisopliae carboxypeptidase A (MeCPA). MeCPA had been genetically engineered to facilitate the removal of polyhistidine tags from the C-termini of recombinant proteins. It has also been used to de-tyrosinate α-tubulin, in vitro, in order to induce high affinity to ethyl-N-phenylcarbamate (EPC) sepharose.

Biochem/physiol Actions

Carboxypeptidase as isolated from bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by beta-phenylpropionate and indole acetate.

Unit Definition

One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.

Preparation Note

Treated with phenylmethylsulfonyl fluoride to eliminate trypsin and chymotrypsin activity. Dialyzed and recrystallized: aqueous suspension with toluene added.

Analysis Note

Protein determined by E1%/278

Safety Information

• Pictograms: GHS08
• Signal Word: Danger
• Hazard Statements: H334
• Hazard Classifications: Resp. Sens. 1
• Storage Class Code: 10 - Combustible liquids
• WGK: WGK 2
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable
• Personal Protective Equipment: dust mask type N95 (US), Eyeshields, Gloves