Welcome to LookChem.com Sign In|Join Free

CAS

  • or
Carboxypeptidase A (CPA) is an enzyme that catalyzes the cleavage of amino acids from a protein at the C-terminus of a polypeptide chain. It is originally isolated from the bovine pancreas and has a molecular mass of 34 kDa, consisting of about 300 amino acids. The enzyme's activity depends on the metal at the catalytic site, with Zn2+ and some Co2+-containing CPAs exhibiting peptidase function, while esterase function has been seen by CPAs containing a variety of divalent d-block metals. The Carboxypeptidase A-agarose product is prepared by the immobilization of CPA to activated 4% crosslinked beaded agarose, resulting in a suspension with a white appearance.

11075-17-5 Suppliers

Post Buying Request

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier
  • 11075-17-5 Structure
  • Basic information

    1. Product Name: CARBOXYPEPTIDASE A
    2. 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
    3. CAS NO:11075-17-5
    4. Molecular Formula: C4H11NO
    5. Molecular Weight: 0
    6. EINECS: 234-297-5
    7. Product Categories: N/A
    8. Mol File: 11075-17-5.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: 4 °C
    4. Appearance: white/suspension
    5. Density: 1.00 g/mL at 20 °C
    6. Refractive Index: N/A
    7. Storage Temp.: 2-8°C
    8. Solubility: N/A
    9. CAS DataBase Reference: CARBOXYPEPTIDASE A(CAS DataBase Reference)
    10. NIST Chemistry Reference: CARBOXYPEPTIDASE A(11075-17-5)
    11. EPA Substance Registry System: CARBOXYPEPTIDASE A(11075-17-5)
  • Safety Data

    1. Hazard Codes: F,Xn,B,Xi
    2. Statements: 11-38-42-48/20-63-65-67-36-36/37/38
    3. Safety Statements: 36/37-45-62-36-26-23-16-24-22
    4. RIDADR: UN 1294 3/PG 2
    5. WGK Germany: 2
    6. RTECS:
    7. F: 10
    8. HazardClass: N/A
    9. PackingGroup: N/A
    10. Hazardous Substances Data: 11075-17-5(Hazardous Substances Data)

11075-17-5 Usage

Uses

Used in Research Applications:
Carboxypeptidase A is used as a comparison tool for studying the specificity of other enzymes, such as Metarhizium anisopliae carboxypeptidase A (MeCPA). This helps in understanding the differences in their catalytic properties and potential applications.
Used in Protein Engineering:
CPA has been utilized in the genetic engineering process to facilitate the removal of polyhistidine tags from the C-termini of recombinant proteins. This is crucial for the purification and characterization of recombinant proteins in various biotechnological applications.
Used in Cell Biology:
Carboxypeptidase A is used to de-tyrosinate α-tubulin in vitro, which helps in inducing high affinity to ethyl-N-phenylcarbamate (EPC) sepharose. This process is essential for studying the structure and function of tubulin proteins and their interactions with other cellular components.
Used in Digestive System:
As a part of the digestive system, Carboxypeptidase A is used as an enzyme that cleaves amino acids favoring the C-terminal end, as well as certain esters. This enzymatic activity plays a vital role in the breakdown and absorption of proteins in the body.
Used in Enzyme Production:
The Carboxypeptidase A-agarose product, prepared by immobilizing CPA to activated 4% crosslinked beaded agarose, is used in various industrial applications, such as enzyme production, where the immobilized enzyme can be easily separated from the reaction mixture and reused multiple times, making the process more efficient and cost-effective.

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].

Check Digit Verification of cas no

The CAS Registry Mumber 11075-17-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,1,0,7 and 5 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 11075-17:
(7*1)+(6*1)+(5*0)+(4*7)+(3*5)+(2*1)+(1*7)=65
65 % 10 = 5
So 11075-17-5 is a valid CAS Registry Number.

11075-17-5Downstream Products

11075-17-5Related news

Application of CARBOXYPEPTIDASE A (cas 11075-17-5) to a baking process to mitigate contamination of wheat flour by ochratoxin A07/19/2019

This study aimed at evaluating an enzymatic strategy to mitigate ochratoxin A (OTA) exposure via contaminated wheat flour. Firstly, the effect of Rhizopus oryzae and Trichoderma reesei, which are both non-toxigenic microorganisms, on OTA, was evaluated. The mycotoxin ​​was degraded by both fungi...detailed

Cloning, characterization and transmission blocking potential of midgut CARBOXYPEPTIDASE A (cas 11075-17-5) in Anopheles stephensi07/18/2019

Transmission-blocking vaccines (TBV) interrupt malaria parasite transmission and hence form an important component for malaria eradication. Mosquito midgut exopeptidases such as aminopeptidase N & carboxypeptidase B have demonstrated TBV potential. In the present study, we cloned and characteriz...detailed

11075-17-5Relevant articles and documents

Method for synthesizing N-ethylethanolamine by micro-channel reactor

-

Paragraph 0029; 0035-0037; 0043-0045; 0051-0053; 0059-0061, (2020/12/09)

The invention discloses a method for synthesizing N-ethylethanolamine by a micro-channel reactor. The method comprises the steps: adopting a Corning high-flux continuous flow micro-channel reactor, setting the flow velocity of the ethylene oxide aqueous solution to be 36.0-46.0mL/min and the flow velocity of the ethylamine aqueous solution to be 20.0mL/min, and respectively pumping the ethylene oxide aqueous solution and the ethylamine aqueous solution into the reactor to be preheated in a first module, that is, a straight-flow type preheating module, which has the temperature of 25-40 DEG C and is independent from each other; and then respectively making the solution enter a second module, that is, an enhanced mass transfer type mixing module, through an inlet A or an inlet B of the reactor, carrying out mixing reaction for 60-200 seconds at the temperature of 25-40 DEG C, and enabling the mixed liquid after the reaction to flow out from an outlet of the reactor; and collecting the output liquid of the micro-channel reaction device, and carrying out dehydrating to obtain the N-ethylethanolamine. The method has the advantages of short time, high efficiency, few byproducts, safety,stability and controllability, and the synthesized N-ethylethanolamine is suitable for pharmaceutical and chemical intermediates.

Discovery of benzimidazole analogs as a novel interleukin-5 inhibitors

Boggu, Pulla Reddy,Kim, Youngsoo,Jung, Sang-Hun

, (2019/08/12)

A series of novel hydroxyethylaminomethylbenzimidazole analogs 5a-y were synthesized and evaluated for their IL-5 inhibitory activity using pro-B Y16 cell line. Among them, 2-(((4-(cyclohexylmethoxy)-1H-benzo[d]imidazol-2-yl)methyl)amino)butan-1-ol (5e, 94.3% inhibition at 30 μM, IC50 = 3.5 μM, cLogP = 4.132) and 3-cyclohexyl-2-(((4-(cyclohexylmethoxy)-1H-benzo[d]imidazol-2-yl)methyl)amino) propan-1-ol (5k, 94.7% inhibition at 30 μM, IC50 = 5.0 μM, cLogP = 6.253) showed the most potent inhibitory activity. The essential feature of SAR (Fig. 5) indicated that the chromenone ring can be replaced by a benzimidazole ring to maintain the inhibitory activity. In addition, the hydroxyethylaminomethyl group was suitable for the IL-5 inhibitory activity. Moreover, the hydrophobic substituents on carbon play an important role in the IL-5 inhibitory activity of these analogs. However, N-substituted analogs did not improve inhibitory activity. In addition, MTT assay of 5e and 5k with normal B lymphoblasts revealed that they had no significant effects on cell viability.

Hydrogenolysis of Amide Acetals and Iminium Esters

Kadyrov, Renat

, p. 170 - 172 (2017/12/26)

Amide acetals and iminium esters were hydrogenated into amines under very mild reaction conditions over common hydrogenation catalysts. This finding provides a new strategy for the selective reduction of amides. The synthetic utility of this approach was demonstrated by the selective reduction of amides bearing ester and nitrile groups.

METHOD FOR PRODUCING 2-(ALKYLAMINO)ETHANOL COMPOUND

-

Paragraph 0042, (2017/08/24)

PROBLEM TO BE SOLVED: To provide a method for effectively producing a 2-(alkylamino)ethanol compound from a N-alkyldiethanolamine compound. SOLUTION: A method for producing a 2-(alkylamino)ethanol compound in which a N-alkyldiethanolamine compound and an alkylamine compound are reacted under the presence of at least one metal catalyst selected from the group consisting of iron catalyst, copper catalyst, nickel catalyst, cobalt catalyst, palladium catalyst, platinum catalyst, silver catalyst, gold catalyst, osmium catalyst, iridium catalyst, ruthenium catalyst, and rhodium catalyst is provided. SELECTED DRAWING: None COPYRIGHT: (C)2017,JPOandINPIT

Catalytic Hydrogenation for the Preparation of Amines from Amide Acetals, Ketene N,O-Acetals or Ester Imides

-

Paragraph 0153; 0154, (2016/10/04)

The present invention relates to a process for the preparation of amines, comprising the following steps: Reaction of a (i) amide acetal of the general formula (I), or (ii) ketene N,O-acetal of the general formula (II), or (iii) ester imide of the general formula (III) with H2 in the presence of a hydrogenation catalyst, where catalyst and amide acetal or ketene N,O-acetal or ester imide are used in a molar ratio of from 1:10 to 1:100 000 and where a hydrogen pressure of from 0.1 bar to 200 bar is established and where a temperature in the range of from 0° C. to 250° C. is established.

N-Alkylation of Alkylolamines with Alcohols Over Mesoporous Solid Acid–Base Cs–B–Zr Catalyst

Chen, Aimin,Wang, Houyong,Liu, Rui,Bo, Yingying,Hu, Jun

, p. 1182 - 1193 (2016/07/06)

Abstract: The mesoporous solid acid–base Cs–B–Zr mixed oxides were synthesized using the co-precipitation method followed by a subsequent thermal treatment. The catalytic activity of solid Cs–B–Zr mixed oxide was tested for solvent free acid–base catalysed direct alkylolamines with alcohols as green alkylating agent. The effects of Cs/B/Zr ratio, calcination temperature, reaction conditions, and reaction substrate on the catalytic performance of the catalysts were investigated. The XRD, N2 adsorption–desorption, ICP-OES, FT-IR and NH3/CO2-TPD results showed that the mesoporous structure and acid–base properties of the catalysts play important roles in the reaction. A suitable number of acid and basic sites on the catalyst lead to a high activity for the N-alkylation reaction. Graphical Abstract: A direct N-alkylation of amino alcohol with alcohols has been developed using mixed oxide Cs–B–Zr as an acid–base bifunctionalized catalyst.[Figure not available: see fulltext.]

2-(ETHYLAMINO)ETHANOL PRODUCTION METHOD

-

Paragraph 0027, (2015/09/23)

The present invention relates to a production method for 2-(ethylamine) ethanol, including subjecting N-ethyldiethanolamine to a disproportionation reaction in the presence of at least one kind of catalyst selected from the group consisting of a manganese oxide catalyst and an alkali metal hydroxide-supporting zirconium oxide catalyst. According to the present invention, 2-(ethylamino)ethanol can be obtained by subjecting N-ethyldiethanolamine to the disproportionation reaction. 2-(Ethylamino)ethanol is a useful compound to be used in various applications such as a drug, an agricultural chemical, and a functional chemical.

Pyrithione biocides enhanced by zinc metal ions and organic amines

-

, (2008/06/13)

The present invention is directed to a stable, soluble, antimicrobial composition concentrate comprising pyrithione or a pyrithione complex in an amount of from about 0.5% to about 30 weight percent, a zinc source in an amount of from about 0.1% to about 10%, and an organic amine component in an amount of from about 30% to about 80%, said percents being based upon the total weight of the composition concentrate. The invention is also directed to methods of controlling the growth of free-living microorganisms or biofilms using the antimicrobial composition of the invention, and products made using the antimicrobial composition of the invention.

Detritylation of N-tritylamines via a naphthalene-catalyzed lithiation process

Behloul, Cherif,Guijarro, David,Yus, Miguel

, p. 1274 - 1280 (2007/10/03)

The reaction of aliphatic and aromatic secondary and tertiary N-tritylamines 1 with lithium powder and a catalytic amount of naphthalene led to reductive detritylation, affording the corresponding amines 2 in good to excellent yields. The trityl group could selectively be removed in the presence of an allyl or a benzyl group. The detritylation process could successfully be extended to several hydroxy, alkoxy and amino functionalized N-tritylamines. The chemoselectivity between the trityl-nitrogen and the trityl-oxygen bond cleavages was also studied. This methodology represents an efficient deprotection of N-tritylamines under nonacidic reaction conditions.

Analine derivatives as OSC inhibitors

-

, (2008/06/13)

The present invention relates to compounds of formula (I) wherein U, Y, V, W, L, X, A1, A2, A3, A4, A5 and A6 are as defined in the description and claims and pharmaceutically acceptable salts and/or pharmaceutically acceptable esters thereof. The compounds are useful for the treatment and/or prophylaxis of diseases which are associated with 2,3-oxidosqualene-lanosterol cyclase such as hypercholesterolemia, hyperlipemia, arteriosclerosis, vascular diseases, mycoses, parasite infections, gallstones, tumors and/or hyperproliferative disorders, and/or treatment and/or prophylaxis of impaired glucose tolerance and diabetes.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1

What can I do for you?
Get Best Price

Get Best Price for 11075-17-5