Palmiter R D, Gagnon J, Walsh K A
Proc Natl Acad Sci U S A. 1978 Jan;75(1):94-8. doi: 10.1073/pnas.75.1.94.
Ovalbumin mRNA was translated in a reticulocyte lysate. The primary translation product starts with methionine derived from Met-tRNAf. When the nascent polypeptide is about 20 residues long, this methionine is removed. The new NH2-terminal glycine is acetylated from acetyl-CoA when the polypeptide is 44 residues long. The sequence of 35 residues at the NH2 terminus of ovalbumin was determined by automated Edman degradation after a method was devised to prevent acetylation during protein synthesis in the reticulocyte lysate. This sequence is the same as that of secreted ovalbumin and does not resemble the transient "signal peptides" associated with most secretory proteins, including three other egg white proteins synthesized in the same cells as ovalbumin.
卵清蛋白信使核糖核酸在网织红细胞裂解物中进行翻译。初级翻译产物起始于源自甲硫氨酰 - 起始转运核糖核酸的甲硫氨酸。当新生多肽约20个残基长时，这个甲硫氨酸被去除。当多肽长44个残基时，新的氨基末端甘氨酸从乙酰辅酶A接受乙酰基而被乙酰化。在设计出一种方法以防止网织红细胞裂解物中蛋白质合成期间乙酰化之后，通过自动埃德曼降解法确定了卵清蛋白氨基末端35个残基的序列。该序列与分泌型卵清蛋白的序列相同，并且与大多数分泌蛋白相关的短暂“信号肽”不同，包括在与卵清蛋白相同的细胞中合成的其他三种蛋清蛋白。
