胰蛋白酶活性比色测定

Trypsin is a member of the serine protease family. It cleaves proteins and peptides into smaller pieces by hydrolyzing peptide bonds at the carboxyl side of lysine and arginine residues. Trypsin is produced by the pancreas as an inactive trypsinogen and is then secreted into the small intestine, where it is cleaved by enteropeptidase and becomes activated. Trypsin activity aberration is implicated in gastrointestinal disorders such as pancreatitis and intestinal mucosal pathology. ScienCell's Colorimetric Trypsin Activity Assay Kit (TRYP) offers a rapid and sensitive way to determine the trypsin activity in mammalian cell/tissue lysates, serum, plasma and other biological fluid samples. Briefly, trypsin cleaves the substrate and releases p-nitroanilide (pNA), a chromophore that can be measured at 405 nm using a spectrophotometer. Chymotrypsin, another structurally similar serine protease, does not interfere with this assay because it does not cleave the trypsin substrate to release pNA.

胰蛋白酶（Trypsin）属于丝氨酸蛋白酶家族，可通过水解赖氨酸和精氨酸残基羧基侧的肽键，将蛋白质和多肽切割为较小片段。胰蛋白酶由胰腺以无活性的胰蛋白酶原形式合成，并分泌至小肠，在肠激酶的作用下被切割后转化为具有活性的胰蛋白酶。胰蛋白酶活性的异常与多种胃肠道疾病密切相关，如胰腺炎及肠黏膜病变等。

ScienCell 胰蛋白酶活性比色测定试剂盒（TRYP）提供了一种快速且高灵敏度的检测方法，可用于测定哺乳动物细胞/组织裂解液、血清、血浆及其他生物体液样本中的胰蛋白酶活性。其原理为：胰蛋白酶特异性切割底物并释放对硝基苯胺（pNA），该显色基团可在405 nm波长下通过分光光度计进行定量检测。另一种结构相似的丝氨酸蛋白酶——胰凝乳蛋白酶由于不能切割该特异性底物释放pNA，因此不会对本检测产生干扰。