SALIVARY APYRASE OF AEDES-AEGYPTI - CHARACTERIZATION AND SECRETORY FATE
SALIVARY APYRASE OF AEDES-AEGYPTI - CHARACTERIZATION AND SECRETORY FATE
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DOI：
10.1016/0305-0491(84)90081-6
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发表时间：
1984-01-01
影响因子：
2.2
通讯作者：
SPIELMAN, A
中科院分区：
文献类型：
--
作者：
RIBEIRO, JMC;SARKIS, JJF;SPIELMAN, A
Salivary gland homogenates of female adult A. aegypti hydrolyzed ATP and ADP thereby defining an apyrase activity. Activity is divalent cation dependent with an optimum pH of 9.0. ATPase and ADPase activities could not be dissociated, thus, suggesting the presence of a true apyrase enzyme. Apyrase activity is low on the day of emergence but increases to 160 mU per pair of glands on the 2nd day. The site at which mosquitoes probed into warm polyacrylamide gels retains apyrase activity, confirming the secretory fate of this activity.
