Hamdaoui A, Schoofs L, Wateleb S, Bosch L V, Verhaert P, Waelkens E, De Loof A
Faculty of Science Semlalia, Université Cadi Ayyad, Avenue Molay Abdellaah, Marrakech, Boite postale S/15, Morocco.
Biochem Biophys Res Commun. 1997 Sep 18;238(2):357-60. doi: 10.1006/bbrc.1997.7283.
A protease-inhibitor was isolated from mature ovaries of Schistocerca gregaria by a combination of trypsin-affinity chromatography and reverse-phase high performance liquid chromatography. It was characterized by aminoterminal amino acid sequencing using Edman degradation based automated microsequencing and by MALDI-TOF mass spectrometry. The N-terminal sequence (Y)XAEXDELA(A)EEY(Y)Q(Q)X(I)(L)M (X being a Cys, an irregular or modified amino acid) revealed no similarities with any other protease inhibitors isolated from invertebrate or vertebrate source. The 14 kDa inhibitor was found to be heat-stable. It shows potent inhibitory activity toward bovine trypsin and chymotrypsin, but not toward pancreatic elastase. It is likely that the characterized inhibitor will serve as an important tool for understanding its role in insect development.
通过胰蛋白酶亲和色谱法和反相高效液相色谱法相结合，从沙漠蝗成熟卵巢中分离出一种蛋白酶抑制剂。采用基于埃德曼降解的自动微量测序法进行氨基末端氨基酸测序，并通过基质辅助激光解吸电离飞行时间质谱法对其进行表征。其N端序列（Y）XAEXDELA（A）EEY（Y）Q（Q）X（I）（L）M（X为半胱氨酸、不规则或修饰氨基酸）与从无脊椎动物或脊椎动物来源分离出的任何其他蛋白酶抑制剂均无相似性。发现这种14 kDa的抑制剂具有热稳定性。它对牛胰蛋白酶和胰凝乳蛋白酶具有强大的抑制活性，但对胰腺弹性蛋白酶没有抑制活性。这种已表征的抑制剂可能会成为理解其在昆虫发育中作用的重要工具。
