Gyang F N, Poole B, Trager W
Mol Biochem Parasitol. 1982 Apr;5(4):263-73. doi: 10.1016/0166-6851(82)90034-2.
An acid peptidase that degrades hemoglobin optimally at pH 3.5, a neutral aminopeptidase and an alkaline endopeptidase that acts on an alpha-N-blocked synthetic substrate have been demonstrated in Plasmodium falciparum in culture. The enzymes were shown to be distinct by anion exchange chromatography, gel filtration on Sephadex G-200 and isoelectric focusing. The activities of the acid peptidase and the aminopeptidase were inhibited by antimalarial compounds.
在体外培养的恶性疟原虫中已证实存在一种在pH 3.5时能最佳降解血红蛋白的酸性肽酶、一种中性氨肽酶以及一种作用于α-N-封闭合成底物的碱性内肽酶。通过阴离子交换色谱法、Sephadex G-200凝胶过滤法和等电聚焦法表明这些酶是不同的。抗疟化合物可抑制酸性肽酶和氨肽酶的活性。