Pancreatin
(Synonyms: 胰酶) 目录号 : GC32412
Pancreatin (Pancrelipase, Pancreatic enzymes), are commercial mixtures of amylase, lipase, and protease. They are used to treat malabsorption syndrome due to pancreatic problems.
Cas No.:8049-47-6
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Pancreatin (Pancrelipase, Pancreatic enzymes), are commercial mixtures of amylase, lipase, and protease. They are used to treat malabsorption syndrome due to pancreatic problems.
| Cas No. | 8049-47-6 | SDF | |
| 别名 | 胰酶 | ||
| Canonical SMILES | [Pancreatin] | ||
| 分子式 | 分子量 | ||
| 溶解度 | DMSO : 5 mg/mL ;Water : < 0.1 mg/mL (insoluble) | 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。
Pancreatic enzyme supplementation for patients receiving enteral feeds
Nutr Clin Pract 2011 Jun;26(3):349-51.PMID:21508176DOI:10.1177/0884533611405537.
Background: Pancreatic enzyme supplementation is an important part of management for a number of gastrointestinal conditions. For patients who are unable to swallow Pancreatin capsules or granules, enteral feeding tubes can be used to administer the pancreatic enzyme. This presents challenges given the unique format of the pancreatic enzyme supplements, with common problems including tube blockage and loss of the enzyme's effect. Methods and results: A novel technique is described for administration of pancreatic enzyme via feeding tubes. For gastrically placed tubes, this involves opening the Pancreatin capsules and suspending the enzyme microspheres in thickened acidic fluid (such as the mildly thickened or "nectar-thick" fruit juice used for dysphagia) for delivery into the feeding tube. This technique minimizes tube blockage by preventing the enzyme from clumping in the tube. For jejunally placed tubes, enzyme microspheres can be crushed and activated with sodium bicarbonate before flushing into the tube, or the activated enzyme mixture can be added to enteral feeds. Conclusions: Pancreatic enzyme supplementation can continue while patients receive enteral feeding. Using the described technique can help to avoid tube blockage and maintain optimal enzyme activity.
The Procyanidin C1-Dependent Inhibition of the Hydrolysis of Potato Starch and Corn Starch Induced by Pancreatin
Molecules 2021 Oct 11;26(20):6121.PMID:34684702DOI:10.3390/molecules26206121.
Procyanidins are contained in various foods, and their effects on starch hydrolysis have been reported. In Japan, black soybeans, which contain a trimeric procyanidin, procyanidin C1 (proC1), are cooked with rice and used to prepare dumplings. In this study, the effects of proC1 on the pancreatin-induced formation of reducing sugars and starch hydrolysis were studied using potato starch and corn starch. ProC1 inhibited both reactions; the inhibition was greater in potato starch than corn starch when added to heated potato starch and corn starch. When heated with proC1, its inhibitory effects decreased, especially in potato starch, suggesting the important role of proC1 itself for the inhibition of potato starch hydrolysis. ProC1 also inhibited the hydrolysis when added to heated, longer amylose (average molecular weight: 31,200), and the inhibition decreased when heated with the amylose. On the other hand, proC1 could not inhibit the hydrolysis when added to heated, shorter amylose (average molecular weight: 4500), but could when heated with the amylose, suggesting the important role of the degradation products of proC1 for the inhibition. We discuss the mechanism of the proC1-dependent inhibition of amylose hydrolysis, taking the molecular weight into account.
Pancreatin enhanced erosion of and macromolecule release from 2,2-bis(2-oxazoline)-linked poly(epsilon-caprolactone)
J Control Release 2003 Jan 17;86(2-3):213-22.PMID:12526818DOI:10.1016/s0168-3659(02)00372-3.
The degradation and erosion of solvent cast films and injection molded bars prepared from poly(epsilon-caprolactone) (PCL) and 2,2'-bis(2-oxazoline) linked poly(epsilon-caprolactone) (PCL-O) were evaluated in simulated gastric fluid (SGF) (pH 1.2, pepsin present) and in simulated intestinal fluid (SIF) (pH 7.5, Pancreatin present). After incubation of the polymer films (10 mg) and bars (70 mg) in the medium, the resulting decrease in molecular weight (degradation) was determined by size exclusion chromatography and the weight loss of the preparations was measured. In addition, the effect of Pancreatin on FITC-dextran (MW 4400) release from PCL and PCL-O microparticles, prepared by w/o/w double emulsion technique, was studied. No degradation or weight loss was observed for either PCL or PCL-O films in SGF (12 h incubation, 37 degrees C). When compared to PBS pH 7.4, Pancreatin hardly enhanced the weight loss of PCL films and bars. In contrast, Pancreatin enhanced substantially erosion of PCL-O films and bars. Unlike PCL preparations, the PCL-O preparations showed surface erosion in SIF. Pancreatin increased considerably FITC-dextran release from both PCL and PCL-O microparticles. In conclusion, the present results demonstrate the enzyme sensitivity of the novel PCL-O polymer. In addition, the results show that Pancreatin present in intestinal fluid may substantially affect drug release from PCL based preparations.
Differences in In Vitro Properties of Pancreatin Preparations for Pancreatic Exocrine Insufficiency as Marketed in Russia and CIS
Drugs R D 2020 Dec;20(4):369-376.PMID:33211277DOI:10.1007/s40268-020-00326-z.
Background: Pancreatic enzyme-replacement therapy (PERT), provided as Pancreatin to patients with pancreatic exocrine insufficiency (PEI), is considered an essential substitute for the pivotal physiological function the pancreas fulfills in digestion. PEI involves a reduction in the synthesis and secretion of pancreatic enzymes (lipase, protease, amylase), which leads to an inadequate enzymatic response to a meal and consequently to maldigestion and malabsorption of nutrients. The efficacy of PERT is strongly dependent on enzyme activity, dissolution, and Pancreatin particle size. Objective: The physiological properties of eight Pancreatin preparations (nine batches; five different brands) available in Russia and CIS (Commonwealth of Independent States: Armenia, Azerbaijan, Belarus, Kazakhstan, Kyrgyzstan, Moldova, Russia, Tajikistan, Uzbekistan) were investigated. Methods: The lipase activity, dissolution, and particle size distribution of samples from multiple batches of Pancreatin of different strengths were measured. Results: Regarding lipase activities, all Pancreatin preparations except Micrazim庐 matched the labeled content. Considerable differences were observed in particle size and dissolution. Conclusion: Pancreatin preparations available in Russia and CIS demonstrate product-to-product and batch-to-batch variability regarding the measured properties of lipase activity, dissolution, and particle size. This may impact the efficacy of PERT and therefore clinical outcomes.
Pancreatin as a source of hospital-acquired salmonellosis
Br Med J 1972 May 13;2(5810):376-8.PMID:5063375DOI:10.1136/bmj.2.5810.376.
Two babies with fibrocystic disease of the pancreas acquired hospital infection with Salmonella agona after treatment with commercial Pancreatin prepared from pig pancreas obtained from abattoirs in Britain.