AUSTEN K F
Immunology. 1960 Apr;3(2):152-73.
A comparative study which differentiates the chloroform inducible esterase activity of human serum from plasmin is presented. Although both esterase activities have a similar pH optimum against p-toluene sulfonyl L-arginine methyl ester, they differ in, at least, six other respects. The proenzyme of the chloroform inducible esterase activity is destroyed by heating at 56° for 30 minutes or by reducing the pH to 2.3, whereas plasminogen is stable to such treatment. The chloroform inducible esterase activity is resistant to soybean trypsin inhibitor while plasmin is mostly inhibited. Activity against N-acetyl L-tyrosine ethyl ester is induced by chloroform, but plasmin is inactive against this substrate. On the other hand, plasmin splits casein but the chloroform preparation does not. Pretreatment of serum with an antigen-antibody precipitate greatly diminishes the chloroform inducible esterase activity but not the streptokinase inducible activity. Evidence is presented which suggests that the chloroform inducible esterase activity consists of two components: one is predominantly active against p-toluene sulfonyl L-arginine methyl ester and is probably not affected by the immune precipitate; the other is more active against N-acetyl L-tyrosine ethyl ester than against p-toluene sulfonyl L-arginine methyl ester, is removed by exposing serum to immune precipitate and bears a significant resemblance to the activated first component of complement. Peptone inducible esterase activity, like that induced by chloroform, arises from a heat and acid labile precursor, is active against p-toluene sulfonyl L-arginine methyl ester and N-acetyl L-tyrosine ethyl ester, is not inhibited by soybean trypsin inhibitor, does not digest casein and is partially removed by exposing serum to the immune precipitate before peptone activation. The esterase activity taken up from serum by the immune precipitate, like that induced by chloroform or peptone, arises from a heat labile precursor, is active against p-toluene sulfonyl L-arginine methyl ester and N-acetyl L-tyrosine ethyl ester, is not inhibited by soybean trypsin inhibitor, and does not digest casein. In view of the evidence that chloroform, peptone and antigen-antibody activate a similar, if not identical, proesterase, which is distinct from plasminogen, the possible role of this enzymic activity in histamine release is considered.
本文介绍了一项比较研究，该研究区分了人血清中氯仿诱导的酯酶活性与纤溶酶。尽管两种酯酶活性对甲苯磺酰-L-精氨酸甲酯具有相似的最适pH值，但它们至少在其他六个方面存在差异。氯仿诱导的酯酶活性的酶原在56℃加热30分钟或pH值降至2.3时被破坏，而纤溶酶原对这种处理稳定。氯仿诱导的酯酶活性对大豆胰蛋白酶抑制剂有抗性，而纤溶酶大多被抑制。氯仿可诱导对N-乙酰-L-酪氨酸乙酯的活性，但纤溶酶对该底物无活性。另一方面，纤溶酶可分解酪蛋白，但氯仿制剂不能。用抗原-抗体沉淀物预处理血清可大大降低氯仿诱导的酯酶活性，但不降低链激酶诱导的活性。有证据表明，氯仿诱导的酯酶活性由两个成分组成：一个主要对甲苯磺酰-L-精氨酸甲酯有活性，可能不受免疫沉淀物的影响；另一个对N-乙酰-L-酪氨酸乙酯的活性比对甲苯磺酰-L-精氨酸甲酯的活性更高，通过将血清暴露于免疫沉淀物中而被去除，并且与补体的活化第一成分有显著相似性。蛋白胨诱导的酯酶活性，与氯仿诱导的活性一样，来自热和酸不稳定的前体，对甲苯磺酰-L-精氨酸甲酯和N-乙酰-L-酪氨酸乙酯有活性，不受大豆胰蛋白酶抑制剂抑制，不消化酪蛋白，并且在蛋白胨激活前通过将血清暴露于免疫沉淀物中而部分被去除。免疫沉淀物从血清中摄取的酯酶活性，与氯仿或蛋白胨诱导的活性一样，来自热不稳定的前体，对甲苯磺酰-L-精氨酸甲酯和N-乙酰-L-酪氨酸乙酯有活性，不受大豆胰蛋白酶抑制剂抑制，并且不消化酪蛋白。鉴于有证据表明氯仿、蛋白胨和抗原-抗体激活了一种相似（如果不是相同）的前酯酶，该前酯酶与纤溶酶原不同，因此考虑了这种酶活性在组胺释放中的可能作用。
