Chatterjee N K, Kerwar S S, Weissbach H
Proc Natl Acad Sci U S A. 1972 Jun;69(6):1375-9. doi: 10.1073/pnas.69.6.1375.
Initiation of protein synthesis in HeLa cells has been synchronized by exposure of the cells to fluoride. Double-labeling of such cells for short pulses with [(35)S]methionine and a tritiated amino acid, followed by Edman degradation of the puromycin-released nascent peptides, has shown that the percent of N-terminal methionine incorporated compared to total incorporation is significantly higher than the value obtained with any of the other amino acids tested. The results suggest that the bulk of the nascent proteins synthesized in vivo by HeLa cells are initiated with methionine.
通过将HeLa细胞暴露于氟化物,实现了蛋白质合成起始的同步化。用[³⁵S]甲硫氨酸和一种氚标记的氨基酸对这些细胞进行短脉冲双标记,然后对嘌呤霉素释放的新生肽进行埃德曼降解,结果表明,与总掺入量相比,N端甲硫氨酸的掺入百分比显著高于用任何其他测试氨基酸获得的值。结果表明,HeLa细胞在体内合成的大部分新生蛋白质是以甲硫氨酸起始的。