Garcia-Sanchez Alfredo, Cerrato Rosario, Larrasa Jose, Ambrose Nicholas C, Parra Alberto, Alonso Juan M, Hermoso-de-Mendoza Miguel, Rey Joaquin M, Mine Madisa O, Carnegie Patrick R, Ellis Trevor M, Masters Anne M, Pemberton Alan D, Hermoso-de-Mendoza Javier
Infectious Disease Unit, Medicine and Animal Health, University of Extremadura, Campus UEX, Avda. Universidad s/n, 10071 Caceres, Spain.
FEMS Microbiol Lett. 2004 Feb 9;231(1):53-7. doi: 10.1016/S0378-1097(03)00958-3.
A partial amino acid sequence of a serine protease from Dermatophilus congolensis allowed the design of oligonucleotide primers that were complemented with additional ones from previously published partial sequences of the gene encoding the enzyme. The polymerase chain reaction (PCR), using combinations of specific and degenerate oligonucleotide primers, allowed the amplification of a 1738-bp internal fragment of the gene, which was finally characterised by inverse PCR as the first full-length sequenced serine protease gene (nasp) from Dermatophilus congolensis. The deduced amino acid sequence of this enzyme, probably involved in the pathogenesis of dermatophilosis, links it to the subtilisin family of proteases.
来自刚果嗜皮菌的一种丝氨酸蛋白酶的部分氨基酸序列，使得能够设计出寡核苷酸引物，这些引物与先前发表的该酶编码基因部分序列中的其他引物互补。使用特异性和简并寡核苷酸引物的组合进行聚合酶链反应（PCR），能够扩增出该基因的一个1738 bp的内部片段，该片段最终通过反向PCR被鉴定为来自刚果嗜皮菌的首个全长测序的丝氨酸蛋白酶基因（nasp）。该酶的推导氨基酸序列可能与嗜皮菌病的发病机制有关，将其与枯草杆菌蛋白酶家族的蛋白酶联系起来。
