Shepard D V, Moore K G
Eur J Biochem. 1978 Nov 2;91(1):263-8. doi: 10.1111/j.1432-1033.1978.tb20961.x.
A protease, present in Lupinus angustifolius cotyledons on the fifth day after germination and assayable by following the release of amino groups from gliadin has been purified to the degree that the associated protein of the extract is undetectable. The enzyme is capable, under varying conditions, of releasing amino groups from lupin alpha, beta and gamma conglutins and possesses a mean molecular weight, by dodecylsulphate/polyacrylamide gel electrophoresis and Sephadex G-75 gel filtration of 27500 +/- 450. The isoelectric point is 9.0 +/- 0.848 with a pH optimum of pH 4.0 using gliadin as substrate.
一种蛋白酶在狭叶羽扇豆萌发后第5天的子叶中存在，可通过跟踪麦醇溶蛋白中氨基的释放来检测，该蛋白酶已被纯化到提取物中的相关蛋白无法检测到的程度。在不同条件下，该酶能够从羽扇豆α、β和γ球蛋白中释放氨基，通过十二烷基硫酸钠/聚丙烯酰胺凝胶电泳和葡聚糖G-75凝胶过滤测得其平均分子量为27500±450。以麦醇溶蛋白为底物时，其等电点为9.0±0.848，最适pH为4.0。
