CARBOXYPEPTIDASE A

한글명:CARBOXYPEPTIDASE A

카스 번호11075-17-5

상품명:CARBOXYPEPTIDASE A

CBNumberCB1776427

분자식NULL

포뮬러 무게0

MOL 파일Mol file

화학적 성질

밀도	1.00 g/mL at 20 °C
인화점	4 °C
저장 조건	2-8°C
물리적 상태	suspension
색상	하얀색
생물학적 소스	enzyme from bovine pancreas
Specific Activity	≥6units/mL packed gel, 25°C
CAS 데이터베이스	11075-17-5

위험 및 안전 성명

위험품 표기	F,Xn,B,Xi
위험 카페고리 넘버	11-38-42-48/20-63-65-67-36-36/37/38
안전지침서	36/37-45-62-36-26-23-16-24-22
유엔번호(UN No.)	UN 1294 3/PG 2
WGK 독일	2
F 고인화성물질	10

그림문자(GHS)

CARBOXYPEPTIDASE A 화학적 특성, 용도, 생산

화학적 성질
Suspension (white)
용도
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.
정의
An enzyme that catalyzes the cleavage of amino acids from a protein at the C-terminus of a polypeptide chain.
일반 설명
Carboxypeptidase A-agarose product is prepared by the immobilization of carboxypeptidase A, originally isolated from the bovine pancreas, to activated 4% crosslinked beaded agarose.
공업 용도
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.
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].

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