11075-17-5 Usage
Description
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.
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.
11075-17-5Relevant 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.
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.
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.
