CENTA
目录号 : GC47071
A colorimetric β-lactamase substrate
Cas No.:80072-86-2
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
CENTA is a colorimetric cephalosporin substrate for β-lactamases.1,2 Upon hydrolysis by β-lacatamases, CENTA turns from light yellow to chrome yellow, which can be quantified by colorimetric detection at 405 nm as a measure of β-lactamase activity.
1.Jones, R.N., Wilson, H.W., Novick Jr., W.J., et al.In vitro evaluation of CENTA, a new beta-lactamase-susceptible chromogenic cephalosporin reagentJ. Clin. Microbiol.15(5)954-958(1982) 2.Bebrone, C., Moali, C., Rival, S., et al.CENTA as a chromogenic substrate for studying beta-lactamasesAntimicrob. Agents Chemother.45(6)1868-1871(2001)
| Cas No. | 80072-86-2 | SDF | |
| Canonical SMILES | O=C(C(N12)=C(CSC3=CC=C([N+]([O-])=O)C(C(O)=O)=C3)CS[C@]2([H])[C@H](NC(CC4=CC=CS4)=O)C1=O)O | ||
| 分子式 | C21H17N3O8S3 | 分子量 | 535.6 |
| 溶解度 | Methanol: soluble | 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。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.8671 mL | 9.3353 mL | 18.6706 mL |
| 5 mM | 0.3734 mL | 1.8671 mL | 3.7341 mL |
| 10 mM | 0.1867 mL | 0.9335 mL | 1.8671 mL |
| 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。
CENTA as a chromogenic substrate for studying beta-lactamases
Antimicrob Agents Chemother 2001 Jun;45(6):1868-71.PMID:11353639DOI:10.1128/AAC.45.6.1868-1871.2001.
CENTA, a chromogenic cephalosporin, is readily hydrolyzed by beta-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of beta-lactamase-producing strains on agar plates, it should be quite useful for kinetic studies and the detection of the enzymes in crude extracts and chromatographic fractions.
In vitro evaluation of CENTA, a new beta-lactamase-susceptible chromogenic cephalosporin reagent
J Clin Microbiol 1982 May;15(5):954-8.PMID:7047560DOI:10.1128/jcm.15.5.954-958.1982.
CENTA is a newly synthesized, beta-lactamase-labile, chromogenic cephalosporin reagent which changes color from light yellow (lambda maximum ca. 340 nm) to chrome yellow (lambda maximum ca. 405 nm) concomitant with hydrolysis of the beta-lactam ring. This compound offers promise as a diagnostic reagent comparable to other chromogens (PADAC and nitrocefin) for the early detection of beta-lactamase-producing clinical isolates, while retaining some antimicrobial effect against Escherichia coli, Klebsiella spp., Proteus mirabilis, Staphylococcus aureus, and non-enterococcal Streptococcus spp. CENTA is relatively unaffected by commonly used microbiological media and human serum.
Study of inhibitory potential and percent inhibition of oil of Syzygium aromaticum and leaves of Ocimum sanctum on ESBL enzyme from Escherichia coli in broilers of Jabalpur
Indian J Pharmacol 2019 Sep-Oct;51(5):337-342.PMID:31831923DOI:10.4103/ijp.IJP_87_17.
Objective: The inhibitory potential and percent inhibition of Syzygium aromaticum oil and fresh juice of Ocimum sanctum leaves on beta-lactamase enzyme of cecal samples of healthy broilers were studied on samples phenotypically positive for extended-spectrum beta-lactamase (ESBL)-producing Escherichia coli. Materials and methods: Four hundred cecal samples screened for ESBL-producing E. coli were collected from 38 poultry sale outlets located in Jabalpur. The effect of S. aromaticum oil and O. sanctum leaves was seen by colorimetric assay with CENTA and Nitrocefin as chromogenic substrate. Results: Mean absorbance value was inversely propotional to the inhibitory potential. Syzigium aromaticum exhibited 0.4±0.02 and 0.41±0.03 mean absorbance value, 28 per cent and 27 per cent of inhibition with CENTA and Nitrocefin respectively. Ocimum sanctum mean absorbance value and per cent inhibition with CENTA and Nitrocefin was 2.03±0.02 and 10.0 ; 1.97±0.06 and 10.0 respectively (p>0.05) showing non- significant difference in CENTA and Nitrocefin activity. Tazobactum (100 μM) as standard control exhibited a mean absorbance value of 0.12 ± 0.01 and 0.13 ± 0.01 and percent inhibition of 99.88 and 98 against CENTA and Nitrocefin, respectively. Combination of Ocimum sanctum and Syzigium aromaticum showed range of 1.69±0.05 to 1.90±0.08 1.61±0.06 to 1.92±0.08 of absorbance value with per cent inhibition of 14 to 15.9 with CENTA and Nitrocefin respectively. Conclusion: The results depicted that the inhibition of beta-lactamase enzyme activity with S. aromaticum oil was higher than that of O. sanctum leaf juice, and combination of both the herbs showed not much difference in activity.
Flexible loops of New Delhi metallo-β-lactamase modulate its activity towards different substrates
Int J Biol Macromol 2020 Apr 28;158:104-115.PMID:32353499DOI:10.1016/j.ijbiomac.2020.04.219.
Two accessory loop regions that are present in numerous variants of New Delhi metallo-β-lactamases (NDM) are important for the enzymatic activity. The first one is a flexible loop L3 that is located near the active site and is thought to play an important role in the catalytic process. The second region, Ω loop is located close to a structural element that coordinates two essential zinc ions. Both loops are not involved in any specific interactions with a substrate. Herein, we investigated how the length and hydrophobicity of loop L3 influence the enzymatic activity of NDMs, by analyzing mutants of NDM-1 with various deletions/point mutations within the L3 loop. We also investigated NDM variants with sequence variations/artificial deletions within the Ω loop. For all these variants we determined kinetic parameters for the hydrolysis of ampicillin, imipenem, and a chromogenic cephalosporin (CENTA). None of the mutations in the L3 loop completely abolished the enzymatic activity of NDM-1. Our results suggest that various elements of the loop play different roles in the hydrolysis of different substrates and the flexibility of the loop seems necessary to fulfill the requirements imposed by various substrates. Deletions within the Ω loop usually enhanced the enzymatic activity, particularly for the hydrolysis of ampicillin and imipenem. However, the exact role of the Ω loop in the catalytic reaction remains unclear. In our kinetic tests, the NDM enzymes were inhibited in the β-lactamase reaction by the CENTA substrate. We also present the X-ray crystal structures of the NDM-1, NDM-9 and NDM-12 proteins.
Chromosome-specific molecular organization of maize (Zea mays L.) centromeric regions
Proc Natl Acad Sci U S A 1998 Oct 27;95(22):13073-8.PMID:9789043DOI:10.1073/pnas.95.22.13073.
A set of oat-maize chromosome addition lines with individual maize (Zea mays L.) chromosomes present in plants with a complete oat (Avena sativa L.) chromosome complement provides a unique opportunity to analyze the organization of centromeric regions of each maize chromosome. A DNA sequence, MCS1a, described previously as a maize centromere-associated sequence, was used as a probe to isolate cosmid clones from a genomic library made of DNA purified from a maize chromosome 9 addition line. Analysis of six cosmid clones containing centromeric DNA segments revealed a complex organization. The MCS1a sequence was found to comprise a portion of the long terminal repeats of a retrotransposon-like repeated element, termed CENTA. Two of the six cosmid clones contained regions composed of a newly identified family of tandem repeats, termed CentC. Copies of CENTA and tandem arrays of CentC are interspersed with other repetitive elements, including the previously identified maize retroelements Huck and Prem2. Fluorescence in situ hybridization revealed that CentC and CENTA elements are limited to the centromeric region of each maize chromosome. The retroelements Huck and Prem2 are dispersed along all maize chromosomes, although Huck elements are present in an increased concentration around centromeric regions. Significant variation in the size of the blocks of CentC and in the copy number of CENTA elements, as well as restriction fragment length variations were detected within the centromeric region of each maize chromosome studied. The different proportions and arrangements of these elements and likely others provide each centromeric region with a unique overall structure.