Relative synthesis of cardiac contractile proteins. Evidence for synthesis from the same precursor pool.
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.
D000199:Actins / Q000096:biosynthesis* / Q000302:isolation & purification; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008297:Male; D009206:Myocardium / Q000378:metabolism*; D009218:Myosins / Q000096:biosynthesis* / Q000302:isolation & purification; D010477:Perfusion; D014335:Tropomyosin / Q000096:biosynthesis* / Q000302:isolation & purification
D000199:Actins; D000596:Amino Acids; D014335:Tropomyosin; D009218:Myosins