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Characterization of all the lipolytic activities in pancreatin and comparison with porcine and human pancreatic juices.
Biochimie ( IF 3.9 ) Pub Date : 2019-07-06 , DOI: 10.1016/j.biochi.2019.07.004
Amal Salhi 1 , Sawsan Amara 2 , Pascal Mansuelle 3 , Rémy Puppo 3 , Régine Lebrun 3 , Brigitte Gontero 4 , Ahmed Aloulou 5 , Frédéric Carrière 4
Affiliation  

Porcine pancreatic extracts (PPE), also named pancreatin, are commonly used as a global source of pancreatic enzymes for enzyme replacement therapy in patients with exocrine pancreatic insufficiency. They are considered as a good substitute of human pancreatic enzymes and they have become a material of choice for in vitro models of digestion. Nevertheless, while the global PPE contents in lipase, protease and amylase activities are well characterized, little is known about individual enzymes. Here we characterized the lipase, phospholipase, cholesterol esterase and galactolipase activities of PPE and compared them with those of porcine (PPJ) and human (HPJ) pancreatic juices. The phospholipase to lipase activity ratio was similar in PPJ and HPJ, but was 4-fold lower in PPE. The galactolipase and cholesterol esterase activities were found at lower levels in PPJ compared to HPJ, and they were further reduced in PPE. The enzymes known to display these activities in HPJ, pancreatic lipase-related protein 2 (PLRP2) and carboxylester hydrolase/bile salt-stimulated lipase (CEH/BSSL), were identified in PPJ using gel filtration experiments, SDS-PAGE and LC-MS/MS analysis. The galactolipase and cholesterol esterase activities of PPE indicated that PLRP2 and CEH/BSSL are still present at low levels in this enzyme preparation, but they were not detected by mass spectrometry. Besides differences between porcine and human enzymes, the lower levels of phospholipase, galactolipase and cholesterol esterase activities in PPE are probably due to some proteolysis occurring during the production process. In conclusion, PPE do not provide a full substitution of the lipolytic enzymes present in HPJ.

中文翻译:

表征胰酶中的所有脂解活性,并与猪和人胰液进行比较。

猪胰腺提取物(PPE),也称为胰酶,通常被用作胰腺酶的全球来源,用于外分泌型胰腺功能不全患者的酶替代治疗。它们被认为是人胰酶的良好替代品,它们已成为体外消化模型的选择材料。然而,尽管脂肪酶,蛋白酶和淀粉酶活性中的总PPE含量已得到很好的表征,但对单个酶知之甚少。在这里,我们表征了PPE的脂肪酶,磷脂酶,胆固醇酯酶和半乳糖脂酶的活性,并将其与猪(PPJ)和人(HPJ)胰液中的脂肪进行比较。在PPJ和HPJ中,磷脂酶与脂肪酶的活性比相似,但在PPE中则低4倍。与HPJ相比,PPJ中的半乳糖脂酶和胆固醇酯酶活性较低,而在PPE中它们进一步降低。在PPJ中使用凝胶过滤实验,SDS-PAGE和LC-MS鉴定了已知在HPJ中显示这些活性的酶,胰脂肪酶相关蛋白2(PLRP2)和羧酸酯水解酶/胆盐刺激脂肪酶(CEH / BSSL)。 / MS分析。PPE的半乳糖脂酶和胆固醇酯酶活性表明,该酶制剂中PLRP2和CEH / BSSL的含量仍然很低,但未通过质谱法检测到。除了猪和人的酶之间的差异外,PPE中较低的磷脂酶,半乳糖脂酶和胆固醇酯酶活性可能是由于生产过程中发生的一些蛋白水解作用所致。综上所述,
更新日期:2019-11-18
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