论文部分内容阅读
分别从健康和患病长毛对虾（Ｐｅｎａｅｕｓｐｅｎｉｃｉｌａｔｕｓ）肌肉提取一种酸性磷酸酶（ＡＣ－Ｐａｅ，ＥＣ．３．１．３．２．），进一步用硫酸铵分级分离，ＳｅｐｈａｄｅｘＧ－２００柱纯化，经聚丙烯酰胺凝胶电泳，并于ＢｅｃｋｍａｎＤＵ－８Ｂ紫外分光光度计扫描为单一区带酶液。该酶紫外吸峰在２８０ｎｍ处，荧光激发峰在２８４ｎｍ处，发射峰在３４７ｎｍ处。酶的分子量为７３０００道尔顿，等电点为４．７酶水解对硝基苯磷酸二钠（ＰＵＰＰ）最适ｐＨ为４．５，最适温度４０℃。健康虾与病虾酶的活化能分别为４１．０３ｋＪ／ｍｏｌ·Ｌ和４５．７８ｋＪ／ｍｏｌ·Ｌ，米多常数ｋｍ值分别为０．８０×１０－４ｍｏｌ／Ｌ和１．４３×１０－４ｍｏｌ／Ｌ。重金属离子Ｃｕ２＋，Ｈｇ２＋，有机溶剂甲醇，乙醇，乙二醇等对ＡＣＰａｓｅ有明显的抑制作用。
An acidic phosphatase (AC-Pae, EC.3.1.3.2.) Was extracted from the muscle of healthy and diseased Penaeus penicillicus, further fractionated with ammonium sulfate and purified by Sephadex G-200 column. Polyacrylamide gel electrophoresis, and BeckmanDU-8B UV spectrophotometer scanning a single zone with enzyme solution. The enzyme UV peak at 280nm, the fluorescence excitation peak at 284nm, the emission peak at 347nm. The molecular weight of the enzyme was 73000 daltons and the isoelectric point was 4.7. The optimal pH of p-nitrophenyl phosphate disodium (PUPP) was 4.5 and the optimum temperature was 40 ℃. The activation energies of healthy shrimp and shrimp shrimp were 41.03 kJ / mol·L and 45.78 kJ / mol·L, respectively, and the km values of rice multi-constants were 0.80 × 10-4 mol / L and 1.43 × 10- 4mol / L. Heavy metal ions Cu2 +, Hg2 +, organic solvents such as methanol, ethanol, ethylene glycol and other ACPase significantly inhibited.