CARBOXYPEPTIDASE A CAS 11075-17-5

Introduction：Basic information about CARBOXYPEPTIDASE A CAS 11075-17-5, including its chemical name, molecular formula, synonyms, physicochemical properties, and safety information, etc.

CARBOXYPEPTIDASE A Basic information

• Product Name: CARBOXYPEPTIDASE A
• Synonyms: Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase from bovine pancreas;Carboxypeptidase A from bovine pancreas,Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase;Peptidyl-L-amino-acid hydrolase from bovine pancreas;Carboxypeptidase A?Agarose;E.C. 3.4.12.2;E.C. 3.4.2.1;PEPTIDYL-L-AMINO-ACID HYDROLASE;PEPTIDYL-L-AMINO-ACID HYDROLASE TYPE II-PMSF
• CAS: 11075-17-5
• MF: NULL
• MW: 0
• EINECS: 234-297-5
• Mol File: Mol File

CARBOXYPEPTIDASE A Chemical Properties

• density: 1.00 g/mL at 20 °C
• Fp: 4 °C
• storage temp.: 2-8°C
• form: suspension
• color: white
• biological source: enzyme from bovine pancreas
• Specific Activity: ≥6units/mL packed gel, 25°C
• CAS DataBase Reference: 11075-17-5

Safety Information

• Hazard Codes: F,Xn,B,Xi
• Risk Statements: 11-38-42-48/20-63-65-67-36-36/37/38
• Safety Statements: 36/37-45-62-36-26-23-16-24-22
• RIDADR: UN 1294 3/PG 2
• WGK Germany: 2
• F: 10
• Storage Class: 10 - Combustible liquids
• Hazard Classifications: Resp. Sens. 1

CARBOXYPEPTIDASE A Usage And Synthesis

Chemical Properties

Suspension (white)

Uses

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.

Definition

An enzyme that catalyzes the cleavage of amino acidsfrom a protein at the C-terminus of a polypeptidechain.

General Description

Carboxypeptidase A-agarose product is prepared by the immobilization of carboxypeptidase A, originally isolated from the bovine pancreas, to activated 4% crosslinked beaded agarose.

Industrial uses

Carboxypeptidase A(CPA) is an enzyme of the digestive system that is known to cleave amino acids favouring the C-terminal end as well as certain esters. This enzymatic activity depends on the metal at the catalytic site. Zn²⁺ and some Co²⁺-containing CPAs exhibit peptidase function, whilst esterase function has been seen by CPAs containing a variety of divalent d-block metals. CPA has a size similar to CA, consisting of about 300 amino acids and a molecular mass of 34 kDa.

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.

Purification Methods

Carboxypeptidase A is purified by DEAE-cellulose chromatography, activation with trypsin and dialysed against 0.1M NaCl, yielding crystals. It is recrystallised by dissolving in 20 mL of M NaCl and dialysed for 24hours each against the following salts present in 500mL of 0.02M sodium veronal pH 8.0, 0.5M NaCl, 0.2M NaCl and 0.15M NaCl. The last dialysate usually induces crystallisation. If it does not crystallise, then dialyse the last solution against 0.02M sodium veronal containing 0.10M NaCl. Only 2 or 3 recrystallisations are required to attain maximum activity. [Cox et al. Biochemistry 3 44 1964.] Enzyme activity is measured by hydrolysing hippuryl-L-phenylalanine (or phenylacetic acid) and observing the rate of change of optical density at 254nm (reaction extinction coefficient is ~0.592 cm2/Wmole at pH 7.5) [Bergmyer Methods in Enzymatic Analysis (Academic Press) 1 436 1974].