Rizki T M, Rizki R M, Bellotti R A
Mol Gen Genet. 1985;201(1):7-13. doi: 10.1007/BF00397978.
An electrophoretic mobility variant of phenoloxidase in a lz stock of Drosophila melanogaster was identified as the A3 component of the phenoloxidase complex by using two different activators to study enzyme activity-natural activator isolated from pupae and 50% 2-propanol. The structural gene for the A3 proenzyme, Dox-3, was not associated with lz on the X chromosome; it mapped to the right of rdo (53.1) and left of M(2)m in the second linkage group. The lz locus affects the differentiation of the crystal cell, the type of hemocyte that carries prophenoloxidase(s) in paracrystalline form. Alleles of lz lacking paracrystalline inclusions in their hemocytes do not have phenoloxidase activity whereas alleles with paracrystalline inclusions have enzyme activity. The presence of proenzyme in the paracrystalline inclusions was demonstrated by in situ activation with natural activator or propanol followed by incubation in buffered dopa.
通过使用两种不同的激活剂来研究酶活性——从蛹中分离出的天然激活剂和50%的异丙醇,在黑腹果蝇的lz品系中鉴定出一种酚氧化酶的电泳迁移率变体,它是酚氧化酶复合物的A3组分。A3酶原的结构基因Dox-3与X染色体上的lz不相关;它定位于第二连锁群中rdo(53.1)的右侧和M(2)m的左侧。lz基因座影响晶体细胞的分化,晶体细胞是携带副晶形式前酚氧化酶的血细胞类型。血细胞中缺乏副晶内含物的lz等位基因没有酚氧化酶活性,而具有副晶内含物的等位基因具有酶活性。通过用天然激活剂或丙醇进行原位激活,然后在缓冲多巴中孵育,证明了副晶内含物中存在酶原。