Peptide nature of two mosquito natriuretic factors.
Peptide nature of two mosquito natriuretic factors.
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两种蚊子利尿钠因子的肽性质。
DOI：
10.1152/ajpregu.1986.250.3.r328
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Beyenbach,KW
中科院分区：
文献类型：
--
作者：
Petzel,DH;Hagedorn,HH;Beyenbach,KW
埃及伊蚊头部生理盐水提取物的高压液相色谱(HPLC)得到三个组分(总共108个)，它们影响分离的马氏伊蚊小管的跨上皮电压和/或液体分泌。在这项研究中，我们研究了这些馏分中活性物质的物理和化学性质。凝胶过滤层析表明，这三个组分的相对分子质量在1900到2700之间。为了测试它们的热稳定性，这些组分在110天内反复冷冻和解冻，而没有失去生物活性。在100摄氏度下煮沸5分钟，未能显著降低它们在分离的马氏管中的生物学效应。相比之下，用蛋白水解酶混合物--链霉酶处理后，这三种酶的活性都被破坏了。组分I不再使体外灌流的马氏管跨上皮电压去极化，组分II和组份III完全失去刺激液体分泌和影响跨上皮电压的能力。我们的结论是，我们的高效液相分离产生了一组由三个极性小分子多肽组成的异质性基团。它们的生物学活性在马氏管中的表达依赖于完整的多肽键。
High-pressure liquid chromatography (HPLC) of saline extracts of Aedes aegypti heads yields three fractions (from a total of 108) that affect transepithelial voltage and/or fluid secretion in isolated Aedes Malpighian tubules. In this study we investigated the physical and chemical nature of the active materials in these fractions. Gel-filtration chromatography revealed that the molecular weights of the three fractions were between 1,900 and 2,700. To test their thermostability the fractions were repeatedly frozen and thawed over a period of 110 days without loss of biological activity. Boiling at 100 degrees C for 5 min failed to significantly reduce their biological effects in isolated Malpighian tubules. In contrast, treatment with the proteolytic enzyme mixture, pronase, destroyed activity in all three. Fraction I no longer depolarized the transepithelial voltage of in vitro perfused Malpighian tubules, and fractions II and III completely lost their ability to stimulate fluid secretion and to affect transepithelial voltage. We conclude that our HPLC isolation yields a heterogeneous group of three polar low-molecular weight peptides. Expression of their biological activities in Malpighian tubules depends on intact peptide bonds.