Maccioni R B, Arechaga J
Exp Cell Res. 1986 Nov;167(1):266-70. doi: 10.1016/0014-4827(86)90224-7.
Transglutaminase (TG) has been examined in different stages of preimplantation mouse embryogenesis. The specific activity of this enzyme in the soluble cellular fraction increases 2-fold from 2-cell embryos to 8-cell morulae and 4-fold from 2-cell embryos to blastocyst. The same developmental profile was seen when either N,N'-dimethylcasein or endogenous substrates were used in the TG assay. Using high-speed supernatants from different stage embryos as a source of enzyme and [3H]putrescine as acyl acceptor, the major acyl donor components were tubulin and a high molecular weight (HMW) cross-linkage product, as assessed by electrophoresis and immunoblotting. When either assembled or monomeric cytoskeleton proteins were compared as substrates, microtubules were the best acyl donors. These studies indicate that TG activity is modulated during the changing demands of blastomeres for microtubule cytoskeleton in early embryogenesis.
已对小鼠植入前胚胎发育不同阶段的转谷氨酰胺酶（TG）进行了检测。该酶在可溶性细胞组分中的比活性从2细胞胚胎到8细胞桑椹胚增加了2倍，从2细胞胚胎到囊胚增加了4倍。当在TG测定中使用N，N'-二甲基酪蛋白或内源性底物时，观察到相同的发育模式。以不同阶段胚胎的高速上清液作为酶源，以[3H]腐胺作为酰基受体，通过电泳和免疫印迹评估，主要的酰基供体成分是微管蛋白和高分子量（HMW）交联产物。当比较组装的或单体的细胞骨架蛋白作为底物时，微管是最好的酰基供体。这些研究表明，在早期胚胎发育中，随着卵裂球对微管细胞骨架需求的变化，TG活性受到调节。
