Seligman J, Shalgi R
Department of Human Genetics, Sackler School of Medicine, Tel Aviv University, Ramat Aviv, Israel.
J Reprod Fertil. 1991 Nov;93(2):399-408. doi: 10.1530/jrf.0.0930399.
Thiol (SH) oxidation to disulphides (SS) is thought to be involved in sperm chromatin condensation and tail structure stabilization, which occur during maturation of spermatozoa. Previously developed procedures, using the fluorescent labelling agent monobromobimane (mBBr), enabled us to study the thiol-disulphide status of spermatozoa. Electrophoretic separation of labelled sperm proteins from the caput and cauda regions showed that during maturation thiol oxidation occurs in many protein fractions from the tail and that the magnitude of oxidation differs between proteins. Among the protein bands, one major band (MPB), probably a dense fibre constituent, is quantitatively prominent. N-Ethylmaleimide (NEM) or mBBr alkylation (of intact spermatozoa) changes the mobility of the caput MPB, but not that of the cauda MPB. The results indicated that the altered mobility of MPB is mainly due to a change in its shape, possibly resulting from the alkylation of a few critical SH groups. Epididymal fluid proteins contain both SH and SS. The thiol and disulphide content of the various epididymal proteins appears similar, although some diminution in fluorescence is seen in epididymal fluid proteins from the cauda region as compared with those from the caput region. The prominent changes in thiol status occur in the spermatozoa.
硫醇（SH）氧化为二硫化物（SS）被认为与精子染色质浓缩和尾部结构稳定有关，这些过程发生在精子成熟期间。先前开发的使用荧光标记剂单溴代双马来酰亚胺（mBBr）的程序，使我们能够研究精子的硫醇 - 二硫化物状态。对来自附睾头和附睾尾区域的标记精子蛋白进行电泳分离表明，在成熟过程中，尾部的许多蛋白质组分中都发生了硫醇氧化，并且不同蛋白质的氧化程度不同。在蛋白质条带中，一条主要条带（MPB），可能是一种致密纤维成分，在数量上很突出。N - 乙基马来酰亚胺（NEM）或mBBr烷基化（对完整精子）会改变附睾头MPB的迁移率，但不会改变附睾尾MPB的迁移率。结果表明，MPB迁移率的改变主要是由于其形状的变化，这可能是由于几个关键SH基团的烷基化所致。附睾液蛋白同时含有SH和SS。各种附睾蛋白的硫醇和二硫化物含量似乎相似，尽管与附睾头区域的附睾液蛋白相比，附睾尾区域的附睾液蛋白荧光略有减弱。硫醇状态的显著变化发生在精子中。
