Klinkert M Q, Felleisen R, Link G, Ruppel A, Beck E
Zentrum für Molekulare Biologie, University of Heidelberg, F.R.G.
Mol Biochem Parasitol. 1989 Mar 1;33(2):113-22. doi: 10.1016/0166-6851(89)90025-x.
We have constructed cDNA clones containing the complete nucleotide sequences coding for two highly antigenic Schistosoma mansoni adult worm proteins, Sm31 and Sm32. The predicted amino acid sequence of Sm31 shows significant homology to mouse, rat and human cathepsin B. The nucleotide sequence of Sm32 is identical to that reported by others for S. mansoni "haemoglobinase'. The different nucleotide sequences demonstrate the existence of two different proteolytic enzymes, both of which are synthesised in the form of precursor molecules. Structural homology of the schistosome cathepsin B to the mammalian ones indicates that the mature protein is processed from a propeptide. The calculated molecular weight of haemoglobinase of 47,000 suggests that post-translational processing is also involved in generating an active protease.
我们构建了cDNA克隆，其包含编码两种高度抗原性曼氏血吸虫成虫蛋白Sm31和Sm32的完整核苷酸序列。Sm31的预测氨基酸序列与小鼠、大鼠和人类组织蛋白酶B显示出显著的同源性。Sm32的核苷酸序列与其他人报道的曼氏血吸虫“血红蛋白酶”的序列相同。不同的核苷酸序列表明存在两种不同的蛋白水解酶，二者均以前体分子的形式合成。血吸虫组织蛋白酶B与哺乳动物组织蛋白酶B的结构同源性表明成熟蛋白是从前肽加工而来的。计算得出的血红蛋白酶分子量为47,000，这表明翻译后加工也参与产生活性蛋白酶。
