The 26 kD protein recognized on rat cauda epididymal sperm by monoclonal antibody 4E9 has internal peptide sequence that is identical to the secreted form of epididymal protein E.
The 26 kD protein recognized on rat cauda epididymal sperm by monoclonal antibody 4E9 has internal peptide sequence that is identical to the secreted form of epididymal protein E.
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单克隆抗体 4E9 在大鼠附睾精子尾部识别的 26 kD 蛋白具有与附睾蛋白 E 的分泌形式相同的内部肽序列。
DOI：
10.1002/(sici)1098-2795(199703)46:3
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Hamilton,DW
中科院分区：
文献类型：
--
作者：
Xu,W;Ensrud,KM;Hamilton,DW
针对大鼠附睾精子尾部的去污剂提取物产生的MAb 4E9识别在精子尾部而不是头部的精子尾部的质膜上发现的26 kD糖蛋白（摩尔等人，1994年）。它还识别一种附睾分泌的蛋白质，该蛋白质已被证明是蛋白质E（Xu和汉密尔顿，1996）。据认为，分泌的蛋白质成为与精子，但一直没有生化证据之间的分泌和膜蛋白的分子身份。在本报告中，已通过反相HPLC纯化了膜形式的抗原。经纯化的蛋白质经溴化氰裂解得到3种肽，也通过反相HPLC纯化。其中一种肽产生了34个氨基酸的明确序列，与附睾液中发现的蛋白质的内部肽相同。这是第一个报告显示附睾分泌蛋白和精子质膜蛋白之间的序列一致性。摩尔
MAb 4E9, raised against a detergent extract of rat cauda epididymal sperm, recognizes a 26 kD glycoprotein that is found on the plasma membrane of the sperm tail in cauda, but not caput, sperm (Moore et al., 1994). It also recognizes an epididymissecreted protein that has been shown to be protein E (Xu and Hamilton, 1996). It is felt that the secreted protein becomes associated with sperm, but there has been no biochemical evidence of molecular identity between the secreted and membrane proteins. In this report, the membrane form of the antigen has been purified by reverse phase HPLC. Cyanogen bromide cleavage of the purified protein yielded 3 peptides that were purified, also by reverse phase HPLC. One of the peptides yielded an unambiguous sequence of 34 amino acids that is identical to an internal peptide of the protein found in epididymal fluid. This is the first report showing sequence identity between an epididymis-secreted protein and a protein of the sperm plasma membrane. Mol.