Yamamoto S, Ikai H, Uesugi T, Horie A, Hirai Y
Faculty of Pharmaceutical Sciences, Okayama University, Japan.
Biol Pharm Bull. 1995 Mar;18(3):454-6. doi: 10.1248/bpb.18.454.
We have previously reported that a novel enzyme, L-2,4-diaminobutyrate decarboxylase (DABA DC), which is responsible for the formation of 1,3-diaminopropane, occurs in two Acinetobacter species. The present study extends this observation to additional Acinetobacter species and strains (6 reference strains and 30 clinical isolates). Furthermore, the DABA DC protein was detected in every strain by Western blot analysis with the antiserum against the enzyme purified from A. baumannii ATCC 19606. However, only the DABA DCs in the A. calcoaceticus and Acinetobacter genospecies 3 in addition to A. baumannii strains strongly cross-reacted with the antiserum, suggesting antigenic heterogeneity among the DABA DC proteins in Acinetobacter species. Therefore, immunological testing of the DABA DC protein may provide an additional method for differentiating and identifying Acinetobacter strains.
我们之前报道过，一种负责生成1,3 - 二氨基丙烷的新型酶——L - 2,4 - 二氨基丁酸脱羧酶（DABA DC），存在于两种不动杆菌属细菌中。本研究将这一观察结果扩展至其他不动杆菌属细菌和菌株（6株参考菌株和30株临床分离株）。此外，通过用针对从鲍曼不动杆菌ATCC 19606纯化的该酶的抗血清进行蛋白质印迹分析，在每一株菌株中都检测到了DABA DC蛋白。然而，除了鲍曼不动杆菌菌株外，只有醋酸钙不动杆菌和不动杆菌属基因种3中的DABA DC与该抗血清发生强烈交叉反应，这表明不动杆菌属细菌中DABA DC蛋白存在抗原异质性。因此，对DABA DC蛋白进行免疫学检测可能为不动杆菌菌株的鉴别和鉴定提供一种额外的方法。
