Pruslin F H, Rodman T C
Exp Cell Res. 1983 Mar;144(1):115-26. doi: 10.1016/0014-4827(83)90446-9.
Following treatment with Triton X/1 M NaCl/2-mercaptoethanol, mouse sperm heads are divested of protamines and other basic proteins; the residual structure is one in which the general morphological organization of the decondensed chromatin and the nuclear boundaries are conserved [1]. In this study, the protein complement of that residual structure has been characterized and subdivided into two sets: 1. Those that are sperm-unique, including constituents of the sperm head that may be intrinsically nuclear (or extra-nuclear, but exceedingly adherent to the nuclear envelope). 2. Those that display corresponding electrophoretic properties and immunologic cross-reactivity with proteins of similarly treated mouse somatic cell nuclei. Among the latter are proteins of molecular weight 52, 63 and 69 kD, two of which (63 and 69 kD) appear to be homologous to polypeptides of somatic nuclear envelope/pore complex lamina. Absence from sperm nuclei of the third of the characteristic predominant triplet of somatic nuclear lamina polypeptides of mammalian cells, here designated 67 kD, indicates cell-type variation in these structures. On the other hand, the identification of homologous polypeptides in the sperm and somatic complements suggests that those are specific instances of conservation and may represent the paternal contribution to the pool of polypeptides for assembly of the envelopes of the pronuclei of the one-cell embryo.
用曲拉通X/1M氯化钠/2-巯基乙醇处理后，小鼠精子头部的鱼精蛋白和其他碱性蛋白被去除；剩余结构中，解聚染色质的一般形态组织和核边界得以保留[1]。在本研究中，已对该剩余结构的蛋白质组成进行了表征，并将其分为两组：1. 精子特有的蛋白质，包括可能本质上属于细胞核（或核外，但与核膜紧密相连）的精子头部成分。2. 那些与经类似处理的小鼠体细胞细胞核蛋白具有相应电泳特性和免疫交叉反应性的蛋白质。后者包括分子量为52、63和69kD的蛋白质，其中两种（63和69kD）似乎与体细胞核膜/核孔复合体片层的多肽同源。哺乳动物细胞体细胞核层多肽特征性主要三联体中的第三种（此处命名为67kD）在精子核中不存在，这表明这些结构存在细胞类型差异。另一方面，精子和体细胞成分中同源多肽的鉴定表明，这些是保守的特定实例，可能代表父本对单细胞胚胎原核包膜多肽组装库的贡献。
