Huang W Y, Chirala S S, Wakil S J
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030.
Arch Biochem Biophys. 1994 Oct;314(1):45-9. doi: 10.1006/abbi.1994.1410.
We have cloned and sequenced the cDNA encoding the chicken fatty acid synthase. Based on the nucleotide-derived amino acid sequence of the chicken synthase, the N-terminal sequences are highly conserved among animal species, suggesting that translation of the animal synthases initiates with the same ATG codon. Like other fatty acid synthases, the NH2-terminal sequence of the chicken enzyme is blocked. We have isolated and purified the blocked NH2-terminal peptide from a tryptic digest of chicken synthase and have established that the blocking group is an acetyl group. The sequence of the native tryptic peptide confirmed the cDNA-derived amino acid sequence and suggested that all animal synthases begin with this homologous sequence. We developed simple procedures that can be used to isolate and characterize any blocked NH2-terminal peptide.
我们已经克隆并测序了编码鸡脂肪酸合酶的cDNA。根据鸡合酶的核苷酸推导氨基酸序列,其N端序列在动物物种中高度保守,这表明动物合酶的翻译起始于相同的ATG密码子。与其他脂肪酸合酶一样,鸡酶的NH2端序列被封闭。我们从鸡合酶的胰蛋白酶消化物中分离并纯化了被封闭的NH2端肽,并确定封闭基团是乙酰基。天然胰蛋白酶肽的序列证实了cDNA推导的氨基酸序列,并表明所有动物合酶都始于这个同源序列。我们开发了简单的程序,可用于分离和鉴定任何被封闭的NH2端肽。