Chymotrypsin
(Synonyms: Chymotrypsin A) 目录号 : GC66092
Chymotrypsin (Chymotrypsin A) 是一种由胰腺产生的丝氨酸蛋白酶（serine protease）。Chymotrypsin 在芳香氨基酸的羧基侧切割蛋白质链。
Cas No.:9004-07-3
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Chymotrypsin (Chymotrypsin A) is a serine protease produced by the pancreas. Chymotrypsin cleaves protein chains at the carboxyl side of aromatic amino acids[1][2].
| Cas No. | 9004-07-3 | SDF | Download SDF |
| 别名 | Chymotrypsin A | ||
| 分子式 | 分子量 | ||
| 溶解度 | DMSO : 50 mg/mL (Need ultrasonic) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
The pharmacology of Chymotrypsin administered by inhalation
Br J Pharmacol Chemother 1960 Jun;15(2):304-12.PMID:13850540DOI:10.1111/j.1476-5381.1960.tb01249.x.
The ability of Chymotrypsin to reach the limits of the bronchial tree has been studied in cats receiving the enzyme by inhalation as a very fine powder. For this purpose derivatives of Chymotrypsin were used which had been labelled with a fluorescent molecule or with [(131)I]. Quantitative measurements of the absorption and distribution of inhaled chymotrypsin- [(131)I] revealed a rapid removal of radioactivity from the lungs over the first 24 hr. and corresponding excretion of labelled inorganic iodide in the urine. High levels of activity were not attained in the blood or thyroid. Subcutaneous administration of labelled enzyme led to more rapid accumulation of radioactivity in the blood and thyroid. Consideration of these and other results leads to the conclusion that, while some enzyme ascends the respiratory tract by ciliary movement of mucus, a substantial part is absorbed into the lungs and the [(131)I] subsequently detached from it.The changes in tidal air accompanying inhalation of labelled trypsin and Chymotrypsin were followed in anaesthetized cats. Trypsin brings about a decrease in tidal air in distinctly lower doses than does Chymotrypsin. Prior administration of mepyramine had an antagonistic effect, and it is suggested that the change in tidal air is essentially the result of bronchial spasm.
The role of amino-terminal alanine in the control of conformation and activity of alpha-chymotrypsin
Eur J Biochem 1982 Dec;129(1):87-92.PMID:7160387DOI:10.1111/j.1432-1033.1982.tb07024.x.
Novel acetylated derivatives of three different three-chained chymotrypsins were prepared from bovine chymotrypsinogen A and their catalytic properties and kinetics of denaturation in urea were compared with those of the corresponding non-acetylated enzymes. Measurements of the Km (apparent) as a function of pH confirmed earlier findings of Valenzuela and Bender [J. Biol. Chem. 248, 4909-4914 (1973)] that the alpha-species of Chymotrypsin is much more sensitive to reversible inactivation at high pH compared to its sister three-chained chymotrypsins, alpha 1 and kappa-chymotrypsin. Similarly, the denaturation rate constants in 8 M urea of alpha-chymotrypsin were much more sensitive to high pH than alpha 1 and kappa-chymotrypsin. The urea denaturation study showed a transition at about pH 8 to a more urea-sensitive form of alpha-chymotrypsin, whereas alpha 1 and kappa-chymotrypsin were relatively insensitive to a change in pH from 6.5 to 10. When the N-terminal Ala149 of alpha-chymotrypsin was acetylated, thus preventing protonation of the N terminus, the active enzyme derivative displayed the same Km (app) vs pH profile as alpha 1 and kappa-chymotrypsin. Urea denaturation studies with this masked derivative also showed that the pH-dependent transition of native alpha-chymotrypsin at pH 8 was eliminated. These results demonstrate that it is the presence of the protonated Ala149 residue in alpha-chymotrypsin that accounts for much of the hypersensitivity of this enzyme species to inactivation and urea denaturation in the pH region 7.5-10.
The differential specificity of Chymotrypsin A and B is determined by amino acid 226
Eur J Biochem 1999 Jan;259(1-2):528-33.PMID:9914536DOI:10.1046/j.1432-1327.1999.00075.x.
The A and B isoforms of the pancreatic serine proteinase, Chymotrypsin are known to cleave substrates selectively at peptide bonds formed by some hydrophobic residues, like tryptophan, phenylalanine and tyrosine. We found, however, that the B forms of native bovine and recombinant rat chymotrypsins are two orders of magnitude less active on the tryptophanyl than on the phenylalanyl or tyrosyl substrates, while bovine Chymotrypsin A cleaves all these substrates with comparable catalytic efficiency. Analysing the structure of substrate binding pocket of Chymotrypsin A prompted us to perform an Ala226Gly substitution in rat Chymotrypsin B. The specificity profile of the Ala226Gly rat Chymotrypsin B became similar to that of bovine Chymotrypsin A suggesting that only the amino acid at sequence position 226 is responsible for the differential specificities of Chymotrypsin A and B isoenzymes.
An enzyme in mast cells with properties like Chymotrypsin
J Exp Med 1959 Sep 1;110(3):451-60.PMID:13798801DOI:10.1084/jem.110.3.451.
Mast cells contain an enzyme which hydrolyzes 3-chloroacetoxy-2-naphthoic acid anilide. By using highly purified mast cells isolated by differential centrifugation in high density sucrose solutions we have been able to study this enzymatic activity in more detail. The enzyme has properties similar to those of Chymotrypsin: Chymotrypsin will hydrolyze the histochemical substrate, and the Chymotrypsin and mast cell activities with this substrate are similarly inhibited by diisopropylfluorophosphate. The mast cell enzyme is capable of hydrolyzing the N-acetyl esters of tryptophan, tyrosine, and phenylalanine, the relative rates of hydrolysis being similar to those seen with Chymotrypsin. A characteristic trypsin substrate, p-toluenesulfonyl arginine methyl ester, is not acted upon by the mast cell enzyme or Chymotrypsin. The pH activity curve of the new cell enzyme is similar to that of Chymotrypsin as determined with N-acetyl-L-tryptophan ethyl ester as substrate.
Active forms of Chymotrypsin C isolated from autolyzed porcine pancreas glands
Biochim Biophys Acta 1985 Oct 4;831(2):249-56.PMID:4041469DOI:10.1016/0167-4838(85)90042-1.
Four active forms of Chymotrypsin C (C1, C2A, C2B, and C3) were isolated from the autolyzed porcine pancreas glands. Their molecular weights were estimated by SDS-polyacrylamide gel electrophoresis to be 29 100 for C1, 26 300 for C2A and C3, and 25 500 for C2B. The kinetic analyses of esterase activity of the enzymes toward Ac-LLeu-OEt and Ac-LPhe-OEt showed that Chymotrypsin C1 hydrolyzed the two substrates more efficiently than did Chymotrypsin C3. Chymotrypsin C1 consisted of chain A (H-Cys-...-Asn-OH, Mr 886) and chain BC (H-Val-...-Lys-OH, Mr 28 200). Chymotrypsin C3 consisted of the two components of C3L and C3S that could be dissociated in the presence of 2.3% SDS. C3L consisted of the chain A and the chain C (H-Ser-...-Lys-OH, Mr 13 600). C3S was the chain B (H-Val-...-Lys-OH, Mr 11 800). These kinetic and chemical analyses show that chymotrypsins C1 and C3 correspond to Chymotrypsin A delta and A alpha, respectively.