Hertner Thomas, Meyer Barbara, Eppenberger Hans M, Mähr Rodolfo
Institute for Cell Biology, Swiss Federal Institute of Technology, CH-8093, Zürich, Switzerland.
Wilehm Roux Arch Dev Biol. 1980 Feb;189(1):69-72. doi: 10.1007/BF00848568.
A new method for isolating the secretion products fromChironomus tentans salivary glands is described. This method has the advantage of allowing the isolation of soluble and undegraded secretion proteins. These proteins have been characterized on SDS-acrylamide gels. Three main proteins (SPI, SPII, and SPIII), with molecular weights of about 1.4, 1.0 and 0.16×10 D were detected. The number of major bands is that expected if, as has been suggested, the three Balbiani rings on the fourth chromosome contain the genes for the secretion proteins. Moreover, the molecular weights of SPI and SPII are in the range expected from the size of Balbiani ring transcripts. In addition we present evidence for a protease which is isolated with the secretion proteins and is fully active only in the presence of reducing agents. This result suggests that a secondary structure, maintained by disulfide bonds, is necessary to prevent proteolytic cleavage of secretion proteins.
本文描述了一种从摇蚊唾液腺中分离分泌产物的新方法。该方法的优点是能够分离出可溶性且未降解的分泌蛋白。这些蛋白已通过SDS-聚丙烯酰胺凝胶进行了表征。检测到三种主要蛋白（SPI、SPII和SPIII），分子量分别约为1.4×10⁶、1.0×10⁶和0.16×10⁶ D。如果如所建议的那样，第四条染色体上的三个巴尔比亚尼环包含分泌蛋白的基因，那么主要条带的数量是预期的。此外，SPI和SPII的分子量在从巴尔比亚尼环转录本大小预期的范围内。此外，我们还提供了一种蛋白酶的证据，该蛋白酶与分泌蛋白一起分离出来，并且仅在还原剂存在时才具有完全活性。这一结果表明，由二硫键维持的二级结构对于防止分泌蛋白的蛋白水解切割是必要的。
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