Ribeiro J M, Sarkis J J, Rossignol P A, Spielman A
Comp Biochem Physiol B. 1984;79(1):81-6. doi: 10.1016/0305-0491(84)90081-6.
Salivary gland homogenates of female adult Aedes 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 second day. The site at which mosquitoes probed into warm polyacrylamide gels retains apyrase activity, confirming the secretory fate of this activity.
成年雌性埃及伊蚊的唾液腺匀浆可水解ATP和ADP，从而确定了一种腺苷三磷酸双磷酸酶活性。该活性依赖二价阳离子，最适pH为9.0。ATP酶和ADP酶活性无法分离，因此表明存在一种真正的腺苷三磷酸双磷酸酶。羽化当天腺苷三磷酸双磷酸酶活性较低，但在第二天增加到每对腺体160 mU。蚊子刺入温暖聚丙烯酰胺凝胶的部位保留了腺苷三磷酸双磷酸酶活性，证实了该活性的分泌命运。
