Yarlett N, Lloyd D
Mol Biochem Parasitol. 1981 May;3(1):13-7. doi: 10.1016/0166-6851(81)90073-6.
The mitochondrial adenosine triphosphatase of the kinetoplastid protozoon, Crithidia fasciculata, is inhibited by oligomycin, venturicidin, triethyltin sulphate, N,N'-dicyclohexylcarbodiimide, leucinostatin, Dio-9 and quercetin, but not spegazzinine or by compounds which interact with the beta-subunit of mitochondrial F1-ATPase (efrapeptin, aurovertin, citreoviridin or 4-chloro-7-nitrobenzofurazan). These results suggest that the F1 portion of the crithidial enzyme has an unusual type of beta-subunit. Further evidence for the atypical nature of this enzyme is provided by the observation that F1-inhibitor proteins from Acanthamoeba castellanii or bovine heart mitochondria do not inhibit the C. fasciculata enzyme activity.
动质体原生动物纤细短膜虫的线粒体腺苷三磷酸酶受寡霉素、抗霉素、硫酸三乙锡、N,N'-二环己基碳二亚胺、亮抑素、Dio-9和槲皮素抑制，但不受斯佩加齐宁或与线粒体F1-ATP酶β亚基相互作用的化合物（埃弗拉肽素、金褐霉素、黄绿青霉素或4-氯-7-硝基苯并呋喃）抑制。这些结果表明，短膜虫酶的F1部分具有一种不寻常类型的β亚基。来自卡氏棘阿米巴或牛心线粒体的F1抑制蛋白不抑制纤细短膜虫酶活性这一观察结果，为该酶的非典型性质提供了进一步的证据。
