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首页> 外文期刊>The Journal of Experimental Biology >Purification and cloning of the salivary nitrophorin from the hemipteran Cimex lectularius
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Purification and cloning of the salivary nitrophorin from the hemipteran Cimex lectularius

机译：半参Cimex lectularius唾液中的氮灵蛋白的纯化和克隆

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Cimex lectularius and Rhodnius prolixus contain salivary nitric oxide (NO) that may help them to feed on their vertebrate hosts by promoting vasodilation and inhibiting platelet aggregation. Salivary NO is associated with heme proteins (nitrophorins) that store and transport NO from the insect salivary glands to the skin of the host. Ln this study, the salivary nitrophorin of Cimex lectularius was purified by DEAE chromatography and reverse-phase high-performance liquid chromatography, The purified nitrophorin had a molecular mass of 32.9 kDa. The DEAE-purified hemoprotein was able to bind NO, and this binding shifted the absorption maximum from 388 nm to 438 nm, The ratio of heme to apoprotein was estimated to be of 1:1. A cDNA clone of 1079 base pairs was sequenced and was found to code for a protein with a molecular mass of 31.7 kDa. The clone sequence was in agreement with the internal peptide sequences obtained from the purified protein. Sequencing of the isolated clone indicates high similarity to several inositol phosphatases; however, no significant similarities emerged when the sequence of C. lectularius nitrophorin was compared with that of R. prolixus nitrophorin, the only other nitrophorin known in insect saliva. Because C. lectularius and R. prolixus belong to two different families of Hemiptera that evolved independently to blood feeding, a case is made for the convergent evolution of these two insect nitrophorins. [References: 15]
机译：Cimex lectularius和Rhodnius prolixus含有唾液一氧化氮（NO），可通过促进血管舒张和抑制血小板聚集来帮助其摄食脊椎动物宿主。唾液中的NO与血红素蛋白（硝化蛋白）相关，后者将NO从昆虫的唾液腺中存储和运输到宿主皮肤。在这项研究中，通过DEAE色谱和反相高效液相色谱法纯化了Cimex lectularius的唾液中的氮荧光素，纯化后的氮荧光素的分子量为32.9 kDa。 DEAE纯化的血蛋白能够结合NO，这种结合将最大吸收从388 nm转移到438 nm。血红素与载脂蛋白之比估计为1：1。对1079个碱基对的cDNA克隆进行测序，发现其编码的蛋白质的分子量为31.7 kDa。克隆序列与从纯化蛋白获得的内部肽序列一致。分离克隆的测序表明与几种肌醇磷酸酶高度相似。然而，当将C.lectularius nitrophorin的序列与R. prolixus nitrophorin的序列进行比较时，并没有明显的相似性。R。prolixus nitrophorin是昆虫唾液中唯一已知的其他nitrophorin。由于C.lectularius和R.prolixus属于半翅目的两个不同家族，它们独立于供血而进化，因此有理由证明这两种昆虫硝化蛋白会聚在一起。 [参考：15]

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