Hosoya M, Miyazaki J, Hirabayashi T
Institute of Biological Sciences, University of Tsukuba, Ibaraki.
J Biochem. 1989 Dec;106(6):998-1002. doi: 10.1093/oxfordjournals.jbchem.a122989.
Smooth muscle of chicken embryonic gizzards has been shown to contain 9 tropomyosin isoforms (E1, E2, E3, E4, E5, E6, E7, E8, and E9) in addition to alpha and beta isoforms (Hosoya et al. (1989) J. Biochem. 105, 712-717). At the early stages of development, the amount of these isoforms was larger than those of alpha and beta isoforms. However, they gradually decreased at later stages and finally disappeared completely after hatching. By using two-dimensional gel electrophoresis and an image analyzing system, we examined the process of tropomyosin accumulation in gizzard smooth muscle development. The accumulation patterns of tropomyosin isoforms and their relative molar ratios to actin in embryonic development were different from those in the stages after hatching. The relative molar ratio of tropomyosin to actin in the thin filament preparation of embryonic gizzards was lower than that of adult, and it gradually increased in the course of embryonic development.
除α和β同工型外,已证明鸡胚砂囊中平滑肌含有9种原肌球蛋白同工型(E1、E2、E3、E4、E5、E6、E7、E8和E9)(细谷等人(1989年)《生物化学杂志》105卷,712 - 717页)。在发育早期,这些同工型的量比α和β同工型的量大。然而,它们在后期逐渐减少,最终在孵化后完全消失。通过使用二维凝胶电泳和图像分析系统,我们研究了原肌球蛋白在砂囊平滑肌发育过程中的积累过程。原肌球蛋白同工型的积累模式及其在胚胎发育过程中与肌动蛋白的相对摩尔比与孵化后阶段不同。胚胎砂囊细肌丝制剂中原肌球蛋白与肌动蛋白的相对摩尔比低于成体,并且在胚胎发育过程中逐渐增加。