Keramaris K E, Stravopodis D, Margaritis L H
Dept of Biology, University of Athens, Greece.
Cell Biol Int Rep. 1991 Feb;15(2):151-9. doi: 10.1016/0309-1651(91)90106-s.
E.S.P. is responsible for the hardening process of the egg-shell at the end of oogenesis (stage 14B) and constitutes a structural component. By immunoblotting, using polyclonal rabbit anti-HRP antibody and anti-rabbit IgG-HRP or Protein A-1251 as second antibody, one major band with MW 38KD on nitrocellulose filter showed positive reaction. We conclude that the E.S.P. is identical to the S38 chorionic protein. Morphological immunogold staining, using pre-embedding procedure, revealed positive reaction in the innermost chorionic layer (ICL) and the endochorion of the eggshell. In addition, electron probe X-ray microanalysis revealed the existence of 37% calcium (explained since the enzyme is Ca2(+)-activated) and 5% iron (explained due to the fact that it is a haemoprotein).
卵壳蛋白（E.S.P.）在卵子发生末期（14B阶段）负责蛋壳的硬化过程，并构成一种结构成分。通过免疫印迹法，使用兔抗辣根过氧化物酶（HRP）多克隆抗体以及抗兔IgG-HRP或蛋白A-125I作为二抗，在硝酸纤维素滤膜上一条分子量为38KD的主要条带显示出阳性反应。我们得出结论，E.S.P.与S38绒毛膜蛋白相同。采用包埋前处理程序的形态学免疫金染色显示，在蛋壳的最内层绒毛膜层（ICL）和内绒毛膜中有阳性反应。此外，电子探针X射线微分析显示存在37%的钙（鉴于该酶是Ca2(+)-激活的，所以可以解释）和5%的铁（由于它是一种血红蛋白，所以可以解释）。
