Murgier M, Pelissier C, Lazdunski A, Lazdunski C
Eur J Biochem. 1976 Jun 1;65(2):517-20. doi: 10.1111/j.1432-1033.1976.tb10368.x.
An enzyme capable of hydrolyzing the substrate L-alanine p-nitroanilide has been found in 18 gram-negative Enterobacteriaceae and Pseudomonas that we tested. This enzyme might be located near the cell surface. Contrastingly we have not detected this activity on colonies of the 8 gram-positive Bacillus that we tested, which suggest a taxonomic value for this test. The aminoendopeptidases found in the various gram-negative bacteria showed similar electrophoretic mobilities and immunological cross-reactivity when tested again Escherichia coli anti-aminoendopeptidase antiserum. The regulation of aminoendopeptidase biosynthesis by the endogenous level of inorganic phosphate that we previously demonstrated in E. coli has been found to exist in all gram-negative organisms tested.
在我们测试的18种革兰氏阴性肠杆菌科细菌和假单胞菌中发现了一种能够水解底物L-丙氨酸对硝基苯胺的酶。这种酶可能位于细胞表面附近。相比之下，在我们测试的8种革兰氏阳性芽孢杆菌菌落上未检测到这种活性，这表明该测试具有分类学价值。当用大肠杆菌抗氨基内肽酶抗血清进行测试时，在各种革兰氏阴性细菌中发现的氨基内肽酶显示出相似的电泳迁移率和免疫交叉反应性。我们之前在大肠杆菌中证明的无机磷酸盐内源性水平对氨基内肽酶生物合成的调节作用，在所有测试的革兰氏阴性生物中均已发现。
