CROSSLINKING OF THE DROSOPHILA CHORION INVOLVES A PEROXIDASE
CROSSLINKING OF THE DROSOPHILA CHORION INVOLVES A PEROXIDASE
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DOI：
10.1007/bf00868677
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发表时间：
1980-01-01
期刊：
影响因子：
--
通讯作者：
MARGARITIS, LH
中科院分区：
文献类型：
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作者：
MINDRINOS, MN;PETRI, WH;MARGARITIS, LH
果蝇绒毛膜含有内源性过氧化物酶活性，其保持无活性直到晚期14，此时其催化绒毛膜蛋白的交联。使用在体外发育的成熟卵泡，可以用过氧化氢诱导过早但正常的交联，并且可以用过氧化物酶抑制剂阻止正常交联。抑制，或过早激活的壳过氧化物酶，允许绒毛膜丝特异性蛋白质的表征，并建立新的标准，用于鉴定蛋壳成分。
The Drosophila chorion contains an endogenous peroxidase activity which remains inactive until late stage 14, when it catalyzes the crosslinking of the chorionic proteins. Using explanted follicles developing in vitro, premature, but otherwise normal crosslinking, can be induced with hydrogen peroxide and normal crosslinking can be prevented with peroxidase inhibitors. Inhibition, or premature activation of the shell peroxidase, allows characterization of chorionic filament specific proteins, and establishes new criteria for the identification of eggshell components.