Evans C D, Schreiber S S, Oratz M, Rothschild M A
Biochem J. 1981 Mar 15;194(3):673-8. doi: 10.1042/bj1940673.
The relative molar synthesis of cardiac contractile proteins has been measured in the perfused heart under control haemodynamic conditions. This synthesis, of myosin heavy chains, individual light chains (1 and 2), actin and tropomyosin, was determined from isolated guinea-pig hearts perfused for 3h simultaneously with constant specific radioactivities and concentrations of [3H]lysine and [3H]phenylalanine. The data strongly suggest that all of the proteins studied were synthesized from the same precursor pools of lysine and phenylalanine, since the ratio of the specific activities of the two labels was the same in all of the proteins. Measurement of molar synthesis of each contractile protein was the same with either labelled amino acid. Under control haemodynamic-perfusion conditions, the relative molar synthesis of the contractile proteins was actin greater than heavy chains greater than light chain 2 greater than light chain 1 greater than tropomyosin.
在对照血流动力学条件下，已对灌注心脏中心脏收缩蛋白的相对摩尔合成量进行了测定。肌球蛋白重链、各个轻链（轻链1和轻链2）、肌动蛋白和原肌球蛋白的这种合成量，是通过用恒定比放射性和浓度的[³H]赖氨酸及[³H]苯丙氨酸同时灌注分离的豚鼠心脏3小时来确定的。数据有力地表明，所有研究的蛋白质都是由赖氨酸和苯丙氨酸的相同前体库合成的，因为两种标记物的比活性在所有蛋白质中都是相同的。用任一标记氨基酸测量每种收缩蛋白的摩尔合成量均相同。在对照血流动力学灌注条件下，收缩蛋白的相对摩尔合成量为肌动蛋白＞重链＞轻链2＞轻链1＞原肌球蛋白。
